2019 Review Questions of Biochemistry (ROY)

Chapter 1 The structure and function of protein

SectionⅠ. Explain the terms
1. Peptide bond: peptide bond is a covalent bond formed between the carboxyl
group of one AA and the amino group of its next AA with elimination of one H2O
molecule. peptide is compound forming by amino acids with peptide bonds.
2. Secondary structure of protein： It refers to the local spatial structure of a certain
peptide segment, that is, the relative positions (3-D arrangement) of backbone atoms
of this peptide segment.
3. pI : The pH at which the protein has zero net-charge is referred to as PI
4. denaturation of protein: Under the influence of some factors, pro spatial
structure is completely destroyed, resulting in the changes of physical and chemical
properties and the loses of their biological functions. This process is called
denaturation of pro.
SectionⅡ. Mono-choice
1) Amino acids differs only in the structure of ( c )
A carboxyl group B amino group C R Group D H atom
2) Which amino acid is not basic amino acid ( d )
A lysine B arginine C histidine D Cysteine
3) Which is not secondary structure of protein ? ( d )
A a-helix B β-pleated sheet C random coil D subunit
4) Which is not the interactions stabilizing the protein tertiary structure? ( a )
A peptide bond B hydrophobic interaction
C ionic interaction D hydrogen bond
5) The chemical bond to maintain primary structure of proteins is ( a )
A. peptide bond B. hydrogen bond
C. hydrophobic bond D. salt bond
6) The chemical bond in charge of maintaining secondary structure of proteins is
( c)
A. salt bridge B. disulfide bond
C. hydrogen bond D. peptide bond
E. hydrophobic interation
7). The chemical bond in charge of the primary structure of proteins is ( d )
A. Salt bridge; B. Disulfide bond
C. Hydrogen bond; D. Peptide bond;
E. hosphodiester bond
Section Ⅲ. Filling the blanks
1. The average content of nitrogen in protein is about________. (16%)
2. Given nitrogen content in a sample of serum is 10g/L, the concentration of proteins
is _______ g/L. (62.5)
3 . The secondary structure of protein is stabilized by________bond .(hydrogen)
4. _________ is the basic building blocks of proteins. (amino acids)
5. Two factors that maintain the stability of hydrophilic colloid of protein are
_________ and _________.(hydration shell, electric repulsion )
6. Adjacent polypeptide chains in β-pleated sheets can be either ____________ or
__________ depending on whether they run in the same direction or in opposite
directions.( parallel antiparalle_)
7. One cysteine can react with another cysteine to form_____________.( disulfide
bond)
Section Ⅳ. Question
1. Why the protein molecule is stable in solution?
Protein solution is a kind of hydrophilic colloid due to the formation of
hydration mantle. The hydrophilic groups of protein contributed on the surface of the
spherical molecule and act with water to form electric double layer which stabling
protein molecule.

2. What is biological change after the protein denatured?

a. The changes of physical and chemical properties and complete loses of biological
functions.
b. decrease in solubility, Solidify and precipitation
c. be susceptible to enzymatic digestion

3. What is the relationship between structure and function of proteins?

a. Primary Structure determines the spatial structure.
b. The spatial structure determines directly the function of pro.
c. The change of pro structure may lead to function alternation .
d. Proteins having similar amino acid sequences demonstrate the functional
similarity
4. What are purification methods based on protein mass and size？
a. Ultracentrifugation is valuable for purifying protein, and determining their
masses based on the centrifugal field generated by high rotational speed.
b. dialysis Dialysis is a process for separating macromlolecules from small
molecules through a semipermeable membrane。
c. Ultrafiltration is a pressure driven membrane separation process on the basis of
molecule size, the molecules larger than the membrane pore size will be retained at
solution. Solvent and small solutes, such as salts and organic compounds with small
molecular weights, pass through the membrane。
4. Gel filtration chromatography separates protein on the basis of their size and
shape using porous beads packed in a column.

5. What are purification methods based on protein loading charges？

a. ion-exchange chromatography: Protein can be purified on the basis of their
charges by ion-exchange chromatography .
b. electrophoresis: Charged particles or molecules in solution will migrate to the
oppositely charged electrode in the electric field. This phenomenon, called
electrophoresis, offers a powerful technique of separating proteins and other
macromolecules, such as DNA and RNA according to their differences in charge types
,charge quantities, and molecular sizes.
c. Agarose electrophoresis and polyacrylamide gel electrophoresis(PAGE) are
among the most powerful and yet conveniently used methods of macromolecular
separation. Isoelectric focusing (IEF),different from general eletrophoresis, separates
proteins in electric field with a pH gradient based on the isoelectric point(PI) of the
separated proteins, if a mixture of protein is electrophoresed through a solution having
a stable pH gradient (the ph smoothly increases from anode and cathode), each protein
will migrate to the position where the pH gradient corresponding to its isoelectric
point and stop there. Protein will be separated according to the differences of
isoelectric points.

Chapter 2 The structure and function of nucleic acids

Ⅰ. Explain the terms
1 . DNA/RNA sequence: The nucleic acid sequence is the sequence of bases
A,C,G,T/U in the DNA or RNA chain.
2. Denaturation of DNA: Dissociation of dsDNA into two ssDNAs is referred to as
denaturation
3. Renaturation of DNA: Two separated complementary DNA strands can rejoin
together to form a double helical form spontaneously when the temperature or pH
returns to the biological range. This process is called renaturation or annealing.
Ⅱ. Mono- choice
1) which is not pyrimidine? (D)
A C (cytosine) B T (thymine) C U (uracil) D A (adenine)
2) Which nucleotide is not basic unit of RNA? (D)
A AMP B TMP C UMP D GMP
3) Which is basic unit of DNA? ( C)
A amino acid B Bases C nucleotide D nucleoside
4) What is the wavelength of maximum absorption by both DNA and RNA ? (A)
A 260 nm B 280 nm C 300 nm D 560 nm
5). The base is found in mRNA but not in DNA is ( E ).
A. A B. C C. G D. T E. U
6. The common composition of DNA and RNA is ( c ).
A. D-ribose B. D-2-deoxyribose C. guanine D. uracil E. thymine
7). Essential of DNA denaturation is ( B ).
A. break of phosphodiester bonds B. rupture of hydrogen bonds
C. break of secondary bonds D. destruction of base stacking
8). The higher the melting temperature of the DNA, the higher its content of ( d )
base pairs.
A. A + T B. A + G C. C + T D. G + C
9). The primary structure of DNA is the sequence of its nucletide residues connected
by ( A )?
A 3’,5’-phosphodiester bonds B hydrogen bonds
C peptide bonds D salt bonds
E disulfide bonds
10). The correct description about Tm is ( A )
A. The temperature at which half of the maximum absorbance value of
DNA at 260nm during heat denaturation
B. The temperature at which maximum absorbance value of DNA at 260nm
during heat denaturation
C. The optimum temperature for DNA synthesis
D. High Tm value is related to low G-C content
E. The temperature to form DNA and RNA hybrid molecule
11). The linkage between nucleotides is (B )
A. 2’,-3’ phosphodiester bond;
B. 3’,-5’ phosphodiester bond
C. 2’,-5’ phosphodiester bond;
D. Hydrogen bond
E. Peptide bond
12). The denaturation of DNA refers to: (C )
A. the destroy of helix
B. the destroy of 3’-5’ phosphodiesterate bond
C. the double strand unfold into two single strands
D. the destroy of spatial structure
E. the destroy of primary structure
13). Which Nucleotide is Not basic unit of DNA? (C )
A. AMP B. TMP
C. UMP D. GMP
D. CMP
(Not)RNA- TMP
Ⅲ. Filling the blanks
1. The nucleic acids are divided into _________ and _____________according to
their pentose. ( deoxyribonucleic acid (DNA) and ribonucleic acid (RNA)
2. Each nucleotide consists of three components____________, ____________ and
____________.( a nitrogenous base, a pentose sugar, and a phosphate group)
3. The Secondary structure of DNA is___________, (double-helical structure )
4. The secondary structure of tRNA is _________. ( cloverleaf)
5. Tertiary structure of tRNA is ________.(reversed L-shape)
6.The linked bond between nucleotides is ____in nucleic acids. (phosphodiester bond)
7.. The temperature at which half of DNA molecules have denatured is called
______________for that DNA.(melting temperature (Tm)
8.. The maximum wavelength of nucleic acids is ________ nm. (260nm)
9. The bases on one strand are paired with the complementary bases on another strand
through H-bonds, namely _______ and ______.(A-T. G-C)
Ⅳ. Question
1). What is the difference in chemical composition between DNA and RNA?

DNA RNA
Base A,G,C,T A,G,C,U
Ribose D-2-deoxyribose D-ribose
Phosphate H3PO4 H3PO4

2. What is Classification of RNA?

 mRNA (messenger RNA): template for protein synthesis.
 tRNA (transfer RNA): AA carrier
 rRNA (ribosomal RNA): place for pro synthesis
 hnRNA (heterogeneous nuclear RNA): precursor of mRNA.
 snRNA(small nuclei RNA): processing and transport of hnRNA.

3. What is the function of 5’-cap and 3’ poly(A) tail of mRNA?

 Enhancing the stability of mRNA
 benefiting transporting from nucleus to cytoplasm
 5’-cap can be recognized by translation initiation factor.

Chapter 3 Enzyme
Ⅰ. Explain the following terms
1). Enzyme active center : Some functional groups are close enough in space to
form a portion called the active center.
2). Enzyme competitive inhibition: Competitive inhibitors are structurally similar to
the substrate and compete reversibly with the normal substrate for the active site of
the same enzyme.
3). Km: Km is the substrate concentration at which the reaction rate isHalf its
maximal veocity. Km value is a characteristic constant of enzyme.
4). Isoenzyme : A group of enzymes that catalyze the same reaction.(do the same
work) but differ from each other in molecular structure, physical-chemical properties.
Ⅱ. Mono- choice
1) Which vitamin can take part in transfer of one carbon unit? (C)
A. vitamin B B. vitamin A C. FH4 D . FH2
2) What is the characteristic constant of enzyme? ( D)
A Optimal temperature B Optimal PH C Vmax D Km
3) what is the active form of vitamin B1 ( B)
A NADH B TPP C FH4 D FMN
4). The effect of competitive inhibitor on enzyme-catalyzed velocity is ( A ).
A. Km increased, Vmax unchanged B. Km decreased, Vmax decreased
C. Km unchanged, Vmax decreased D. Km decreased, Vmax increased
 E. Km decreased, Vmax unchanged
5). The effect of noncompetitive inhibitor on enzyme-catalyzed velocity is ( C ).
A. Km increased, Vmax unchanged B. Km decreased, Vmax decreased
C. Km unchanged, Vmax decreased D. Km decreased, Vmax increased, E.
Km decreased, Vmax unchanged

6). In vivo, which of following vitamins can be converted into NAD+and NADP+?
( D )
A. VitB1 B. VitB2 C. VitB6 D. VitPP
7). About competitive inhibitors, which of the following is NOT true? ( E )
A. Similar to the substrates
B. Bind to the active centre of the enzymes
C. Bind to the enzyme reversibly.
D. Bind to the enzyme by non-covalent bond
E. None of the above
Ⅲ Filling the blanks
1）The reversible inhibition of enzyme can be divided into ________,_________and
_______ .(competitive inhibition, noncompetitive inhibition,uncompetitive inhibition)
2 ） The holoenzyme consists of ____________ and its ____________.(apoprotein,
cofactor)
3 ） The value of Km quantifies the affinity of the enzyme and the substrate . The
larger the Km， the affinity. (the lower)
4) .The features of the enzyme-catalyzed reaction are , , and .
(highly efficiency,highly specifity,highly regulation)
5) The activated form of Vit B1 is in body, and the activated forms of VitPP are
________ and _________.(TPP, NADH, NADPH)
6). Activated forms of VitB2 in vivo are ____________ and ________,. (FAD,FMN)
7). ____________ inhibitor lowers the Vmax of an enzyme without altering Km.
(noncompetitive inhibitor)
8). ____________inhibitor increases the Km of an enzyme without altering Vmax.
(competitive inhibitor)
9).The specificity of enzyme-catalyzed reactions includes ___________,
__________and____________.(absolute specificity, relative specificity,
Stereospecificity )
10). The active center has two essential groups in general ： _________ and
_________. ( binding group,catalytic group)
Ⅳ. Question
1) Describe briefly the factors affecting enzyme-catalyzed reaction.
 enzyme concentration
 substrate concentration
 pH value
 temperature
 inhibitor
 activator
2) Describe the characteristics of enzyme-catalyzed reactions.
 highly efficiency
 highly specifity
 highly regulatory

Chapter 4 Carbohydrate Metabolism

I . Explain the terms:
1. Gluconeogenesis: Formation of new glucose molecules from noncarbohydrate
precursors
2. Cori Cycle: Lactate produced in muscle by glycolysis, is transported to the liver
where it is converted to pyruvate which then enters gluconeogenesis and form
glucose, the glucose then once again is transported in blood circulation to muscle.
II. Filling in the blanks
1. The glycolysis product under aerobic conditions is__________, and the glycolysis
product under anaerobicconditions is_________. (pyruvate, lactate)
2. Gluconeogenesis mainly takes place in the tissue___________. ( liver )
3.___________,____________and__________can act as precursers of
gluconeogenesis. (lactate , glycerol , alanine )
4. In human being, the two tissues_________and ___________ can synthesize
glycogen. (liver, muscle )
5. The two key enzymes for glycogenesis and glycogenolysis are ____________and
______________(Glycogen synthase ,Glycogenp hosphorylase)
6.Pentose Phosphate Pathway can produce two important product including
_________and_______.( Ribose-5-phosphate ,NADPH )
III. mono-choices
1 What kind of carbohydrates can be directly absorbed into human body? (A)
A Monosaccharide B Disaccharide C Oligosaccharides D Polysaccharides
2 The following that does not belong to ketone bodies is: (B)
A acetoacetate B acetate C acetone D β-hydroxybutyrate
3 Ketone Bodies are synthesized in: (C)
A muscle B blood C liver D heart
4 The immediate product of β-oxidation is: (B)
A acetate B acetyl CoA C glycerol D acetone
5. Gluconeogenesis occurs primarily in the _______tissue (A)
A liver B kidney C brain D heart
6 The hormone which can decrease the blood glucose is ( C ).
A Glucagon B Epinephrine C Insulin D Glucocorticoid
7 All the following small molecules can be used to synthsize glucose excep t ( B ).
A Glycerol B NAD+ C Lactate D Alanine
8. The compound which can not be converted into glucose is in animals. ( D ).
A. lactate B. pyruvate C. glycerol D. fatty acid E. glycine
9 The important end products of pentose phosphate pathway are: ( C ).
A.5-phosphate ribose, NADH B.6-phosphate glucose, NADPH
 C. 5-phosphate ribose, NADPH D.6-phosphate fructose, NADPH
E.5-phosphate ribose, FADH2
10 The active form of glucose in glycogen synthesis is: ( D).
A. glucose B. G-6－P C. G-1-P
D. UDPG E.CDPG
11 In the muscle, glucose 6-phosphhate cannot be converted into the following
compounds EXCEPT ( D ).
A. Glycogen B. Acetyl CoA C. Lactate
D. Glucose E. Fructose 6-phosphate
Ⅳ. Question :
1 What are the Roles of glycolysis?
• Easily produces a little amount of ATPs while cell lacking O2
• Nearly every cell can make ATPs by glycolysis;
• glycolysis is Especially useful in strong exercise such as 100m race ;
• For cells without mitochondrium as mature BRC, glycolysis is the sole way to get
energy
2 What are Roles of Krebs Cycle?
• Krebs Cycle Completely oxidize C and H (from sugars, fat and/or amino acids)
to H2O and CO2 producing much energy;
• Krebs Cycle is the hub of intermediary metabolism serving both the catabolic
and anabolic processes;
• It provides precursors for the biosynthesis of glucose, amino acids, nucleotides,
fatty acids, sterols, heme groups, etc.)
3 Compare the different roles of Liver glycogen and Muscle glycogen
 Liver glycogen: buffer for regulating blood glucose levels;
 Muscle glycogen: produces G-6-P for anaerobic ATP synthesis (Glycolysis).)

Chapter 5 Lipid Metabolism

I. Explain the terms
1. Essential Fatty Acids
Linoleic, linolenic and arachidonic acids are called essential fatty acids, because
they cannot be synthesized by the body and must be obtained through diet.
2. Ketone Bodies
Ketone bodies arewater-soluble fuels normally exported by the liver but
overproduced during fasting or in untreated diabetes mellitus, including acetoacetate,
β-hydroxybutyrate, and acetone.
3. Fat mobilization
The triacylglycerol stored in the adipocytes are hydrolyzed by lipases, to
produce free fatty acids (FFA) and glycerol, which are released to the blood, this
process is called fat mobilization

II．Filling in the blanks

1) During times of prolonged starvation, ketone bodies replace glucose as the major
source of energy for many tissues especially_______and _______.(brain, muscle)
2) Four steps of b-oxidation of acyl-CoA are _________,__________,________and
________. (dehydrogenation, hydration, redehydrogenation, thiolysis )
3) Ketone bodies are _______________,___________and_______. (acetoacetate, β-
hydroxybutyrate, and acetone.)
4) Ketone bodies are produced in ______but utilized by _______.(liver, extrahepatic
tissues)
III. Mono-choice
 1. Under condition of starvation, the major fuel for the brain is (   C   ).
A. blood glucose          B. fatty acids
C. ketone bodies          D. amino acids
2. The acetyl CoA required for the synthesis of fatty acids is mainly derived from ( 
E   ).
A. fat mobilization                B. β-oxidation of fatty acids
C. degradation of amino acids     D. glycolysis
E. degradation of glucoses
3. The tissue that cannot go on β-Oxidation of Fatty acids is: (  D  ).
A liver; B lung; C heart; D brain
4. Which is the key enzyme in the regulation of cholesterol synthesis? ( C)
A . HMGCoA synthase B. squalene monooxygenase
C. HMGCoA reductase D. squalene synthase
E. HMGCoA thiolase
5. The carrier for long chain acyl CoA to enter into mitochondria is: ( D ).
A．Citric acid B．Malic acid
C．3-glycerophosphate D．Carnitine
E．ACP
6.Which is the correct sequence of 4 reactions in fatty acids βoxidation? ( C)
A . dehydrogenation, redegydrogenation, hydration, thiolysis
B. thiolysis, dehydrogenation, redegydrogenation, hydration
C. dehydrogenation, hydration, redehydrogenation, thiolysis
D. hydration, dehydrogenation, thiolysis, redegydrogenation
E. dehydrogenation, thiolysis, redegydrogenation, hydration
7. Ketone Bodies can be broken down and utilized in the following tissues but
(D)
A: heart B: muscle C: brain D: liver
Ⅳ Question
• Under which condition fat begin mobilization?
(when blood sugar is low)
• What are the immediate products of β-oxidation?( The acetyl CoA)
• What is Ketone Bodies? (Ketone bodies arewater-soluble fuels normally
exported by the liver but overproduced during fasting or in untreated diabetes
mellitus, including acetoacetate, β-hydroxybutyrate, and acetone).
• Ketone Bodies synthesized where? (liver)
• Ketone Bodies utilized where? (out liver)
• Under what conditions Ketone Bodies synthesized ?
(When blood glucoseis low, because either① exhaustion of other cellular
 carbohydrate stores (glycogen), or② insufficient insulin (type1 diabetes).

Chapter 6 Biological oxidation

I. Explain the terms
1) Biological oxidation
It refers to the process in which chemical substances are completely Oxidized
into H20、ATP and CO2 。
2) Electron transfer chain(Respiratory chain)
It refers to a chain of proteins and coenzymes in the inner membrane of
mitochondria in which 2H are sequentially transferred to O2 to generate H2O。
3) Oxidative phosphorylation
It refers to the process in which ATP synthesis is linked to the oxidation of
NADH and FADH2 by electron transport through respiratory chain.
4) substrate-level phosphorylation
a high energy phosphate substrate directly give its high energy phosphate to ADP
to form ATP， this kind of ATP production，without the role of respiratory chain
of mitochondrum，is called substrate-level phosphorylation
II. Filling in the blank
1) Arrangement of NADH respiratory chain are: , , , and ________.
(NADH— FMN—CoQ---Cyt)
2) Arrangement of succinate respiratory chain are: , , , and _________.
(Succinate---FADH2--—CoQ---Cyt)
3) Tow mobile electron carriers are ________ and _______. (CoQ , CytC)
4) The manners of generating ATP in the body include________and ___________ .
(substrate phosphorylation , Oxidative phosphorylation )
5) There are two respiratory chains in the inner membrane of mitochondria:
_________and ______.(NADH Respiratory chain , succinate respiratory chain.)
III. Mono-choice
1）The characteristics of biological oxidation are: ( D )
A．Hydrogen produced in oxidation combines directly oxygen to form water,
B．No catalysis of enzyme,
C．The reactions takes place in cytoplasm,
D．The energy is released step by step,
E．No regulation by other factors in body and environment.
2) Where are respiratory chain? ( B )
A．The outward of membrane of mitochondria,
B．The interior of membrane of mitochondria,
C．Among membrane of mitochondria,
D．In media of mitochondria,
E．Other p laces.
3) Which compound can NOT be oxidized by NADH-oxidation respiratory chain?
( D )
A．Pyruvate B．Lactate
 C．Malate D．Succinate E．α-katoglutarate

4) The sequence of cytochrome in respiratory chain is: ( C )

A. c----c1----b----aa3----O2 B. c1---- c ----b----aa3----O2
C. b ----c1---- c ----aa3----O2 D. b ---- c ---- c1 ----aa3----O2
E. c---- b ---- c1 ----aa3----O2
5) Which is the inhibitor of complex IV? ( D)
A. RotenoneB. B. Piericidin A
C. Oligomycin D. CO
E. Uncouplers
6) How many coupled sites does NADH ETC have? ( C)
A. 1 B. 2
C. 3 D. 4
E. 5
7 ). Which enzyme ‘function can be inhibited by KCN ? ( A )
A. Cytaa3 B. Cytc1
C. Cytc         D. Cytp450  
D.  Cytb
Ⅳ Question
1) Write down the sequence of NADH respiratory chain.

2) Write down the sequence of succinate respiratory chain.

3) Write down the name of two shuttle systems.

1. Glycerol phosphate shuttle
2. Malate shuttle
4) Write down the mechanism of oxidative phosphorylation regulation.
1. The regulating function of ADP
2. Inhibitors of Oxidative Phosphorylation
(1) Inhibitors of ETC
(2) Uncouplers
(3) ATP synthase inhibitors
3. Hormone
4. mt DNA mutation

Chapter 7 Amino Acid Metabolism

I. Term Explanations
1. Nitrogen balance
The normal state in the adult occurs when degradation of body protein equals
synthesis of new protein. The amount of nitrogen excreted in the urine each day
equals the amount of nitrogen ingested daily.
2. Essential amino acids
These amino acids cannot be synthesized in the body and, therefore, must be
present in the diet in order for protein synthesis to occur. These essential amino
acids are histidine, isoleucine, leucine, lysine, methionine, phenylalanine,
threonine, tryptophan, and valine.
3. Transdeamination
The combined action of an aminotransferase and glutamate dehydrogenase is
referred to as transdeamination.
II. Mono –choice questions
1. The nitrogen atoms of urea produced in the urea cycle are derived from: ( B )
A. nitrate B. ammonia and aspartic acid
C. nitrite D. ammonia
2. Urea cycle converts: ( A )
A. ammonia into a less toxic form
B. ketoacids into amino acids
C. amino acids into keto acids
D. none of these
3. What can be synthesized by Met and Arg metabolism? ( A )
A. polyamine
B. dopamine
C. pyrimidine base
D. urea
4. Which amino acid will be converted to catecholamine? ( D)
A. Tryptophan
B. Glutamic acid
C. Aspartic Acid
D. Tyrosine
5. Protein quality is determined by: (C )
A. the type of amino acid
B. the number of amino acid
C. the number and type of essential amino acid
D. the type of essential amino acid
6. When amino acid take place transamination, what will not be produced? ( C)
A. amino acid
B. α-keto acid
C. NH3
D. pyridoxal phosphate
7. What is the intermediate in TCA and Urea Cycle? ( C )
A. oxaloacetic acid
B. α-ketoglutarate acid
C. fumaric acid
D. citric acid
8. In ornithine cycle, secondary amino group for urea synthesis is derived from (
C ).
A. free ammonia B. glutamine
C. aspartate D. asparagines E. carbamoyl phosphate
9. The major fate of ammonia in the body is: ( C )
A. to synthesize nonessential amino acids B. to synth esize glutamine
C. to synthesize urea D. to synthesize alanine
E. to synthesize nucleotides
10 . The most important role of S-adenosyl methionine ( SAM ) is: ( E )
A. to provide methionine B. to synthesize tetrahydrofolate
C. to synthesize purine nucleotides D. to synthesize pyrimidine nucleotides
E. to supply methyl group
11. About the doner of active methyl group in body, which one is correct? ( E )
A. N5–CH3 –FH4 B. methionine
C. S-adenosyl homocysteine D. N10–CH3 –FH4
E. S-adenosyl methionine(SAM)
12. Which amino acid is nutritionally essential? ( E)
A. Aspartate B. Glutamic acid
C. Alanine D. Tyrosine E. Methionine
13. In the synthesis of urea, one N come from NH3, which of the following amino
acid provide another N for urea? ( B)
A. Pro; B. Asp;
C. Glu; D. Phe; E. Lys
III. Short Answer Questions
1.Describe briefly the sources and outlets of blood ammonia(NH3).
The sources of ammonia: 1. Deamination of amino acid; 2. Absorption in intestine
(urea hydrolysis and Hydrolyses of protein in intestine by bacteria) ; 3.kidney:
Gln deamination
fate of ammonia: 1. Synthesize urea; 2. Synthesize nonessential amino acid; 3.
Synthesize purine and pyrimidine
2. Explain the metabolic pathway of α-keta acid in briefly
There three pathway for α-keta acid metabolism:
 Synthesize nonessential amino acid; α-keta acid can be resynthesized by
transamination.
 α-keta acid can be converted to glucose and acetone body; the leucine and
Lysine will be converted to acetone body uniquely; the others can be
converted to glucose and acetone body.
 Produce energy; α-keta acids will be converted to fatty acids after
decarboxylation; and the later will produce H2O, CO2 and ATP through
oxidation of Fatty Acids
3.Describe the synthesis process of urea.
The synthesis of urea happens in hepatocytes through four steps:
1) The NH4+ generated in liver mitochondria is immediately used, together
with CO2 (as HCO3-), to form carbamoyl phosphate in the matrix;
 2) Carbamoyl phosphate donates its carbamoyl group to ornithine to form
citrulline, with the release of Pi.
3) Aspartate enter the urea cycle and react with citrulline to form arginino-
succinate; The argininosuccinate is then cleaved by argininosuccinase to
form free arginine and fumarate
4) In the last reaction of the urea cycle, the cytosolic enzyme arginase cleaves
arginine to yield urea and ornithine.
4.Describe the process of Glucose-alanine cycle and physiological significance
: The process of Glucose-alanine cycle
1) The amino acid also transfer its α-amino group to pyruvate by the action of
alanine aminotransferase to get alanine.
2) Pyruvate is readily available product of muscle glycolysis.
3) The alanine passes into the blood and travels to the liver. In the cytosol of
hepatocytes, alanine aminotransferase transfers the amino group from alanine
to α-ketoglutarate, forming pyruvate and glutamate.
4) Glutamate can then enter mitochondria, where the glutamate dehydrogenase
reaction releases NH4+.
Physiological significance of Glucose-alanine cycle
1) The use of alanine to transport ammonia from skeletal muscles to the liver is
one example of the intrinsic economy of living organisms.
2) Vigorously contracting skeletal muscles operate anaerobically, producing
pyruvate and lactate from glycolysis as well as ammonia from protein
breakdown.
3) These products must find their way to the liver, where pyruvate and lactate
are incorporated into glucose, which is returned to the muscles, and ammonia
is converted to urea for excretion.

Chapter 8 Nucleotide Metabolism

Section Ⅰ Term Explanations
(1) De novo Synthesis
De novo synthesis of nucleotides begins with their metabolic precursors: amino
acids, ribose 5-phosphate, CO2 and NH3.
(2) Salvage Synthesis
Salvage pathways recycle the free bases and nucleosides released from nucleic
acid breakdown.
Section Ⅱ Filling in the blank
1. A nucleotide is a nucleoside with ________or _______. (one , more phosphates ).
2. Ribose is found in RNA (ribonucleic acid) ； Deoxyribose is found in DNA
(deoxyribonucleic acid).
3. Inosinate (IMP) is the immediate precursor of____ and______. (AMP , GMP)
4. Terminal product of Purine Degradation is uric acid (Urate).
Section III mono –choice questions

1. The end catabolic product of purine nucleotides in human is ( B )

 A. Urea B. Uric acid
C. Creatinine D. Creatine E. -alanine
2. Which of the following is first synthesized in the process of de novo synthesis of
purine nucleotide? ( C)
A. GMP B. AMP
C. IMP D. ATP E. GTP
Section Ⅴ Question
1.What is thel significance of salvage synthesis of purine nucleotide.
• It saves the consumption of energy and some amino acids.
• It is a imperative pathways for some tissues and organs in vivo, such as
brain, marrow and so on.
2. Please compare of the difference between CPS I and CPS II in a living
organism.
Carbamoyl phosphate for pyrimidine synthesis is made by carbamoyl phosphate
synthetase II (CPS II). This is a cytosolic enzyme (whereas CPS I is mitochondrial
and used for the urea cycle) Substrates are HCO3-, glutamine, 2 ATP
Type Cabamoyl phosphate synthetase I (CPS-I) Cabamoyl phosphate synthetase II(CPS-II)
Site Mitochondrion(mt) Cytosol
function Urea synthesis Pyrimidine synthesis
Substrate NH3，CO2 Gln, CO2, ATP

Chapter 9 DNA Replication

Ⅰ. Term Explanations
1. Semi-conservative replication: The two parental strands separate and each strand
serves as a template;Each daughter duplex has one parental strand and one new
strand.
2. Semi-discontinuous replication: DNA polymerase Proceeds in a 5’ to 3’
Direction, the two strands are antiparallel. One strand of DNA is made in the same
direction as the movement of replication fork and made Continuously(leading strand),
whereas the other strand is discontinuously synthesized in Fragments(lagging strand) .
3. Reverse transcription: the process of synthesizing DNA using RNA as a template
and reverse transcriptase as a catalyst.
II. Fill in the blank
1. All DNA polymerases have two basic activities, which are and , the
proofreading activity relies on the activity. (Polymerase activity, 3’-5’ exonuclease
activity , 3’-5’ exonuclease activity )
2. In E.coli, DNA polymerase can be divided into three types. is the primary
enzyme of DNA synthesis, whereas the fills in gaps on lagging strand. (DNA
polymerase III, DNA polymerase I)
3. DNA synthesis is the polymerization of nucleotides. Only if the incoming
nucleotide base pairs with , the DNA polymerase catalyzes the bond formation
between the nucleotide and the 3’ end of the growing strand. A _______made by
primase is required to initiate DNA synthesis.(Template, primer)
4. Replication is very accurate, two mechanisms utilized by DNA polymerase to
ensure the replication fidelity are and . ( Base selection, proofreading)
5. During initiation of DNA replication, DNA polymerase cannot start DNA synthesis
without a primer, which is a short piece of ______, synthesized by a special RNA
polymerase called_______. ( RNA, primase )
6. Semi-continuous replication is referred to_______ strand replicated continuously
and the _______strand replicated discontinuously. (leading strand, lagging strand)
III. Mono-choice
1. Deamination of cytosine gives , this error be corrected by base excision
repair. (A)
A. Uracil can B. Thymine can
C. Uracil can NOT D. Thymine can NOT
E. Guanine can
2. DNA polymerase itself cannot separate the DNA double strands, unzips DNA
duplex to prepare the template. (A)
A. helicase B. Topoisomerase
C. Single strand binding protein D. DnaA E. Primase
3. recognizes DNA lesions that cause large structural changes. (A)
A. Nucleotide excision repair B. Direct repair
C. Base excision repair D. photo repair E. None
4. Which enzyme is not involved in the Base excision repair ? (E)
A. DNA glycosylase B. AP endonuclease
C. DNA polymerase I D. DNA ligase E. DNA photolyase
5. Which of the statements below is wrong ? (E)
A. In DNA replication, when the incoming nucleotide base pairs with the
template, the DNA polymerase catalyze the formation of a phospha-diester
bond.
B. The DNA polymerase requires a DNA template
C. A primer is required by DNA polymerase to start DNA synthesis
D. DNA polymerase I take part in DNA repair
E. DNA polymerase III do NOT have the 3’-5’ exonuclease activity.
6. Which of the following does not participate in DNA replication? (C)
A. helicase B. single strand binding protein
C. transciption factor D. ligase
E. primase
IV． Question
1 List the name and activities of the enzymes involved in DNA replication
There are several protein factors with various enzyme activities in DNA replication
including,

a DNA polymerase: Polymerase activity and 3’-5’ exonuclease activity

(proofreading)
b DNA helicase: Separation of DNA double strands
c Topoisomerase: relieves the topological stress produced by helicase
d Primase: synthesize RNA primers
e Proteins recognize the replication origin
2. A. List at least three DNA repair system.
B. Give an example of DNA damage form and the corresponding repair
manner.
A. Base excision repair, Nucleotide excision repair and Direct repair
B. Example I
Pyrimidine dimers caused by UV. This DNA damage can be repaired by Direct repair
or Nucleotide excision repair
Example II
Deamination of cytosine produces uracil. This error is corrected by base excision
repair.
3. List at least two different features between the prokaryotes and eukaryotes in
DNA replication.
DNA replication is more complex in eukaryotes than that in prokaryotes,
First, the size of DNA in eukaryotes is larger (6 billion bps vs. 4.6 million), so there
are multiple replication origins in eukaryotes in contrast that there is only one origin
in prokaryotes.
Second, the chromosome DNA is linear in eukaryotes whereas it’s circular in
prokaryotes, so in eukaryotes there is a mechanism to solve the End Replication
Problem.
Third, DNA is packaged into nucleosomes in eukaryotic cells, so DNA must be
released from histones before synthesis and repackaged into nucleosomes after
replication.
4. Describe the process of reverse transcription.
Reverse transcription is the process of synthesizing DNA using RNA as a template
and reverse transcriptase as a catalyst.
It includes 3 steps: 1. Production of the first complementary DNA strand from an
RNA template; 2. Hydrolysis of the RNA strand in the DNA-RNA hybrid duplex; 3.
Synthesis of the second cDNA strand from the DNA template.

Chapter 10 RNA Transcription and Chapter 11 protein translaion

I . Term Explanations
1. Promotor: Promoter is the sequence which is recognized and bound by RNA
polymerase
2. Asymmetric transcription ： on the one hand, only the template starnd is used for
the transcription, but the coding strand is not (for a given gene); on the other hand, the
template starnd of different genes does not always locate in the same strand。
3. mRNA splicing: In eukaryotic pre-mRNA processing , the intron is removed
and the two exons precisely linked to produce a matured mRNA molecule.
 4. exon: Exon are the coding sequence that appears in splite gene and primary
transcript;
5. Intron: intron are the noncoding sequences that are transcripted into primary
transcript, and will be cleaved out in the later splicing process
6. degeneracy of codon: a single amino acid is coded for by several different
triplet codons with the exception of Met and Trp which are encoded only by a
single codon AUG and UGG.
7. Condon: an unit consisting of three consecutive nucleotides ,which codes for
a specific amino acid.
8. Anticondon: an unit on tRNA which is complementary to the codon on Mrna
9. Genetic Code Wobble: a less strict specificity in the base pairing of the 5’
base of the anticodon in tRNA allows it to make alternative hydrogen bonding
with the third base of the codon in mRNA beyond the usual G-C and A-U
pairings.
10. S-D sequence: Correct binding of mRNA on ribosome requires alignment of a
pyrimidine-rich sequence on 3'-end of 16S RNA of 30S small subunit with a
purine-rich part of 5'-end of mRNA ,The purine-rich segment - the ribosome-
binding site - is known as the Shine-Dalgarno (S-D) sequence
II. Filling in the blanks
1. The features of genetic codon include_______,________,______,_______and
________.(Universality ,Direction, Commaless, Degeneracy, Wobble)
2. Eukaryotic mRNA posttranscriptional modification processing includes 5’ , 3’
and . ( caping, poly(a)tailing , splicing)
3. There is only kind of prokaryotic RNA pol, while there are kinds of
eukaryotic RNA pols.( one, three )
4. The holoenzyme of E coli RNA pol is composed of ___________and
________. (core enzyme, σ factor)
5. In E. coli, RNA polymerase is composed of two functional parts, namely
________and _______.(core enzyme, σ factor)
6. There are three termination codons in genetic codons, namely _________,
_________ . _________, respectively.（UAA, UAG, UGA）
7. During elongation of a peptide chain, the codons in the mRNA are read in a
_____direction, the growing polypeptide is extended in a__________direction.
( 5‘----3’, N-----C)
8. For protein synthesis, the elongation (ribosomal cycle) stage can be divided into
three steps: _____________, ____________, and ____________.(entrance or
registration,formation of a peptide,translocation)

III. Mono-choice
1．The function of σ subunit of RNA polymerase in Prokaryotes is ( D )
A. to bind DNA template B. to elongates an RNA strand
 C. to unwind DNA strands D. to recognizes initiation site of transcription
2. Which of the following agents inhibits the initiation of RNA synthesis in
prokaryotes by binding to the β-subunit of RNApolymerase? (C )
A. α-Amanitin B. Actinomycin D
C. Rifampin D. Puromycin
3．Which of the following codon serves as start condon? ( D)
A. UAA B. UAG
C. UGA D. AUG
4. In protein synthesis, the initiation (start) codon in mRNA is ( A ).
A. AUG B. UAA
C. UAG D. UGA
5. In most cases, a single amino acid is coded for by several different triplet codons.
This phenomenon is called ( ) of genetic codons. ( A)
A. degeneracy B. wobble
C. universality D. variability
6. Number of genetic codes for encoding 20 standard amino acids is (C)
A. 20 B. 24 C. 61 D. 64
7. Promoter means ( D ).
A. a unit for transcribed fragments
B. transcription origin
C. translation origin
D. a region of DNA template which RNA-pol binds to
E. a sequence being apart from structural gene and enhancing transcription
9. In prokaryote, when transcription, which subunit in RNA-pol takes the role of
binding the DNA template? (E)
A. α B. σ C. ω D. β E. β’
10. If the base sequence in a fragment of the coding strand of DNA is 5′-
ACTACTCAG-3′, corresponding sequence of mRNA produced by transcription is
( E ).
A. 5′-TGATGAGTC-3′ ′-CTGAGTAGT-3′
C. 5′-ACUACUCAG-3′ 5′-UGAUGAGUC-3′
E. 5′-CUGAGUAGU-3′
11. The three stop codon are ( B ).
A. UAA, CAA, UCC B. UAA, UAG, UGA
C. AUG, AGU, AUU D. UCC, UCA, UAC
E. UCG, UGC, UCC
12. The template strand of DNA is 5’-ATTCAG-3 ’ , its transcript is ( D ).
A. 5’ -GACTTA-3’ B. 5’ -CTGAAT-3’
C. 5’ -UAAGUC-3’ D. 5’ -CUGAAU-3’
E. 5’ - TAAGTC-3’
13 .The direction of protein synthesis (polypeptide chain) is ( A ).
A.From N to C B.From 5’ to 3’
C. From C to N D. From 3’ to 5’
E. None of above
14 ． In prokaryote, when transcription, which subunit in RNA-pol takes the role of
recognizing the transcription start site? ( B ).
A. α B. σ C. ω D. β E. β’
15. Which one will be removed in mRNA splicing during the posttranscription
modification? ( A)
A. Intron B. Exon
C. Methylated guanine D. Poly A tail
D. 5’ Cap structure
16. The S-D sequence is on the ( B)
A. 3’ end of 16s-rRNA
B. 5’ end of mRNA
C. 3’ end of 23s-rRNA
D. 3’ end of mRNA
E. 5’ end of 16s-rRNA
IV Question
1. Please compare the similarity and the difference between replication and
transcription.
Similarity: Both processes use DNA as the template (both are guided by a
template); Abide by Base- pairing principle; both have the same polarity in strand
extension (5` to 3`).
Difference
replication transcription
Template double strands single strands
Substate dNTP NTP
Primer yes no
Enzyme DNA polymerase RNA polymerase
Product dsDNA ssRNA ㈠
Base-pair A-T G-C A-U T-A G-C
Mode semiconservative asymmetric
Error Rate proofreading no proofreading
2. Describe briefly the process of post-transcriptional modification of mRNA in
eukaryotic organisms.
1 5’—capping;
2 3’-poly(a) tailing;
3 mRNA splicing.
3．Describe briefly the main features of the genetic code.
1 Universality : All organisms, from virus to human being use nearly the
universal genetic code.
2 Direction: Codons in the coding sequence of mRNA are arranged from 5’ to
3’direction.
3 Commaless: The triplet codons arranged in the coding sequence of mRNA
are commaless,
4 Degeneracy: 18 out of 20 amino acids have more than one codon to specify
 them.
5 Wobble: The codon in mRNA base pairing with the anticodon in tRNA may
not observe the standard base pairing rules
3 Describe briefly the major participants in translation and their functions in
that process.
20 AAs acts as the substrate
mRNA acts as a template
tRNA acts as an adaptor
Ribosomes: acts as the place of protein biosynthesis.
some other enzymes and protein factors:
Aminoacyl-tRNA synthetases: activates the amino acid for protein synthesis
initiation factors，elongation factors，release factors

Chapter 12 Genetic Engineering

Section I Term Explanations
1. DNA cloning
A process for getting an identical DNA molecule copy. A method for identifying
and purifying a particular DNA fragment (clone) of interest from a complex mixture
of DNA fragments, and then producing large numbers of the fragment (clone) of
interest.
DNA cloning = Molecular cloning= Gene cloning = Recombinant DNA
2. plasmid
A plasmid is a small circular DNA found in bacteria that are not part of the
bacterial chromosome. Bacteria carry plasmids because they often have genes that
confer some advantageous characteristic on the bacteria (like antibiotic resistance).
3. Restriction endonuclease
A Restriction Endonucleases will cut both strands of a DNA duplex at a specific
place
4. Gene library (gene bank)
A collection of different DNA sequence from an organism each of which has been
cloned into a vector for ease of purification, storage and analysis.
cDNA libraries: made from cDNA- copy of mRNA
5. Gene vector
It is a tool to be required to carry the DNA fragment of interest into the host cell
for amplify and expressing.
Section Ⅱ Filling in the blank
1. Cleavage site end by restriction endonucleases produce Sticky or Blunt end .
2.Generally getting a target DNA (gene) by Chemical synthesis 、 Gene libraies (or
gene bank) and PCR .
3. PCR consists of three steps : Denaturation、Primer annealing and Elongation .

4.Common cloning vectors inclues Plasmids DNA、bacteriophage DNA 、Virus DNA

and so on.
Section III. Mono-choice
1. Genetic engineering: (D)
1) Is a natural process
2) Only takes place in micro-organisms
3) Happens when cells divide
4) Involves combining DNA from different species
1. Human growth hormone HGH is produced in the pituitary gland. Where is the
gland located? (B)
1) Stomach
2) Brain
3) Intestine
4) Lung
3. Which of the following is not associated with genetic engineering? (A)
1) Translation
2) Transformation
3) Cloning
4) Expression
Section Ⅳ Question
1. List the main steps involved in genetic engineering.
• Getting a target DNA (gene)
• Selecting and constructing gene vector
• Ligation of foreign DNA and vector
• Introduce recombinant DNA into host cell (bacterial cell)
• Screening of recombinant DNA
• Expression of cloning gene
2. what is target DNA(gene)？Write down the major resources of target DNA.
Target DNA---- the DNA of interest
(1) Chemical synthesis
(2) Gene libraies (or gene bank):
-Genomic libraries (G-libraries)
-cDNA libraries(C-libraries)
(3) PCR
3. What is PCR? Simple state the basic principles and process of PCR.
It is a rapid procedure for enzymatic amplification of a specific segment of DNA in
vitro.
PCR consists of three steps :
• Denaturation: 95C, 15-30sec
• Primer annealing: 55 C -62 C, 30sec-2min
• Elongation: 72 C, 1min-10mins
After 20-30 cycles, the original DNA has been amplified a million-fold (100
folds) and billion-fold(1000 folds).

4. What DNA can be used as a vector? What condition is necessary for a

 cloning vector? .
Constructing gene vector from : Plasmids DNA, bacteriophage DNA or Virus DNA.
General features for a gene Vector:
(1) Origin(ori) of replication: autonomously replicating DNA
(2) Selectable markers: such as antibiotic resistance
(3) Multiple cloning sites (MCS) (restriction enzyme sites):  cutting/pasting of
DNA fragments
(4) Easily to be isolated from the host cell
(5) Most are circular, some are linear
Chapter 13 Regulation of Gene Expression
I Term Explanations
1. Genome ： In biology the genome of an organism is its whole hereditary
information and is encoded in the DNA (or, for some viruses, RNA). This includes
both the genes and the non-coding sequences of the DNA.
2. gene expression ：gene expression is to produce mRNA and a biologically active
protein by transcription and translation respectively.
3. zinc finger ： The zinc finger domain is a DNA-binding motif consisting of
specific spacings of cysteine and histidine residues that allow the protein to bind
zinc atoms.
II . Filling in the blanks
1. Gene expression is regulated at different time and stage (temporal specificity and
spatial specificity in cell). So one gene sometimes is silence (gene off ),
sometimes is active (gene on).
2. DNA binding protein includes_________,________,_________and _____ et al.
（transcriptional factor, coactivators, corepressors and RNA polymerase II）
3 ． Gene expression is to produce mRNA and a biologically active _______by
transcription and ________, respectively. (protein translation)
III. Mono-choice
1. Gene structure does not include (C )
A. Chromatin Structure B. promoter structure
C. transcription factors D. histones
2. The homeodomain is ( D )
A. Chromatin B. promoter
C. Zinc Fingers D. a highly conserved domain
3. The HLH transcription factors binding ( A )
A. CAAT box B. TATA box
C. GC box D. transcription start site
4. which can be used to reporter gene assay ( B )
A. the promoter activity B. luciferase
C. DNA-protein binding D. protein-protein interaction
5. which method can not test the DNA-protein binding ( B )
A. gel shift assay B. reporter gene assay
C. Chromatin immunoprecipitation assay D. EMSA

6. Gene expression means ( C).

A. replication and transcription
 B. replication, transcription and translation
C. transcription and translation
D. transcription and post-transcriptional process
E. translation and post-translational process
Section Ⅳ Question :
1. How many Structural Motifs of DNA binding protein?
Homeodomain,
Helix-Loop-Helix (HLH),
Zinc Fingers and Leucine Zipper
2. Describe briefly the methods to study gene regulation.
Methods for detecting the promoter activity,
methods for detecting the DNA-protein binding
and methods for detecting protein-protein interaction.
3. How to detect protein-protein interaction.
GST pull-down,
Co-immunoprecipitation and Co-localization.

Chapter 14 Heme Metaboism

I Filling in the blank
1. The basicl materials of heme synthesis are _________,________and _________.
(succinyl CoA, glycine, Fe2+)
2.The rate-limiting enzyme of heme synthesis is ________, coenzyme of which is
________. (ALA synthase, VitB6)
II. Mono-choice
1. The basic material of heme synthesis are ( E)
A. acetyl CoA, Fe2+ B. globin, Fe2+
C. succinyl CoA, Fe2+ D. acetyl CoA, glycine, Fe2+
E. succinyl CoA, glycine, Fe2+
2. The key enzyme for heme biosynthesis is (B )
A. UPGIII isomeiase B. ALA synthase
C. ALA dehydratase D. Deaminase
E. Heme synthase
III Question :
1 .Describe briefly the difference of free bilirubin and conjuated bilirubin

Difference of two bilirubins

Free bilirubin Conjugated bilirubin
Binding with Glucuronic acid no yes
solubility in water small large
Discharged via kidney no yes
Pass through the membrane of cell yes no