Chapter 2 Micro

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CHAPTER-2

MOLECULES OF LIFE
Water Chemistry
All living organisms are dependent on
water.

The structure of water is the basis for its


unique properties.

The most important property of water is


the ability to form hydrogen bonds.
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Water Chemistry
Within a water molecule, the bonds between
oxygen and hydrogen are highly polar.

Partial electrical charges develop:


- oxygen is partially negative
- hydrogen is partially positive

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Water Chemistry
Hydrogen bonds are?

Hydrogen bonds can form between water


molecules or between water and another
charged molecule.

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Water Chemistry

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Properties of Water
1. Water has a high specific heat.

2. Water has a high heat of vaporization.

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Properties of Water
3. Solid water is less dense than liquid
water.

4. Water is a good solvent.

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Properties of Water
5. Water organizes nonpolar molecules.
- hydrophilic:
-hydrophobic:
- Water causes hydrophobic molecules to
aggregate or assume specific shapes.

6. Water can form ions.


H2O  OH-1 + H+1
hydroxide ion hydrogen ion
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Carbohydrates
Molecules with a 1:2:1 ratio of carbon,
hydrogen, oxygen
-empirical formula: (CH2O)n
-examples: sugars, starch, glucose

C – H covalent bonds hold much energy


Carbohydrates are good energy storage
molecules.
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Carbohydrates
Glucose
-a monosaccharide – single sugar
-contains 6 carbons
-very important in energy storage
-fructose is a structural isomer of glucose
-galactose is a stereoisomer of glucose

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Carbohydrates

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Carbohydrates

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Carbohydrates
Disaccharides
-2 monosaccharides linked together by
dehydration synthesis
-used for sugar transport or energy
storage
-examples: sucrose, lactose, maltose

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Carbohydrates

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Carbohydrates
Polysaccharides
-long chains of sugars
-used for energy storage
-plants use starch; animals use glycogen
-used for structural support
-plants use cellulose; animals use chitin

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Carbohydrates

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Nucleic Acids
Two types: DNA and RNA

Functions: specialized for the storage,


transmission, and use of genetic
information

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Nucleic Acids
Nucleic acids are polymers of nucleotides.
-nucleotides:
sugar + phosphate + nitrogenous base
-sugar is deoxyribose in DNA
or ribose in RNA
-Nitrogenous bases include
-purines: adenine and guanine
-pyrimidines: thymine, cytosine, uracil
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Nucleic Acids

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Nucleic Acids
DNA
-nucleotides connected by phosphodiester
bonds
- double helix: 2 polynucleotide strands
connected by hydrogen bonds
-polynucleotide strands are complementary
-genetic information is carried in the
sequence of nucleotides
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Nucleic Acids
RNA
-contains ribose instead of deoxyribose
-contains uracil instead of thymine
-single polynucleotide strand
-functions:
-read the genetic information in DNA
-direct the synthesis of proteins

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Nucleic Acids
Other nucleotides
-ATP: adenosine triphosphate
-primary energy currency of the cell

-NAD+ and FAD: electron carriers for many


cellular reactions

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nucleotides and nucleic acids
There are four different nitrogen-
containing bases in DNA and RNA:

A = adenine
C = cytosine
G = guanine

T = thymidine in DNA
U = uracil in RNA
Molecules of Life:

Remember - in DNA:

A always pairs with T

G always pairs with C

pairing is due to
hydrogen bonding
nucleotides and nucleic acids

Information flow in a cell:

DNA  RNA  protein

DNA = library RNA = photocopy

Each amino acid of a protein is encoded by


a group of 3 DNA nucleotides (a codon)
nucleotides and nucleic acids

DNA: ATG CCG TCC ACG GGA TTT TAA

RNA: AUG CCG UCC ACG GGA UUU UAA

Protein: met pro ser thr gly phe stop


(start)
Molecules of Life:
proteins

Composed of amino acids joined together


in a specific sequence for each particular
protein
-- only 20 normally occurring amino acids
Proteins
Protein functions include:
1. enzyme catalysts
2. defense
3. transport
4. support
5. motion
6. regulation
7. storage
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Proteins
Proteins are polymers of amino acids.

Amino acids
-20 different amino acids
-joined by dehydration synthesis
-peptide bonds form between adjacent
amino acids

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Proteins

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Proteins
Amino acid structure
-central carbon atom surrounded by
-amino group
-carboxyl group
-single hydrogen
-variable R group

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Proteins
The shape of a protein determines its function.
-primary structure – sequence of amino acids
-secondary structure – interaction of groups in
the peptide backbone
-a helix
-b sheet

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Proteins
Protein structure (continued)
-tertiary structure – folded shape of the
polypeptide chain
-quaternary structure – interactions between
multiple polypeptide subunits

Protein folding is aided by chaperone


proteins.
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Proteins
Denaturation is a change in the shape of a
protein, usually causing loss of function.
-may involve complete unfolding
-caused by changes in the protein’s
environment
-pH
-temperature
-salt concentration
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Proteins

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Lipids
Lipids are a group of molecules that are
insoluble in water.

A high proportion of nonpolar C – H bonds


causes the molecule to be hydrophobic.

Two main categories:


-fats (triglycerides)
-phospholipids
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Lipids
Triglycerides (fats)
-composed of 1 glycerol + 3 fatty acids
Fatty acids are long hydrocarbon chains
which may be
-saturated (solids at room temperature)
-unsaturated (liquids at room
temperature)
-polyunsaturated (Liquids at room
temperature)
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Lipids
Triglycerides
-an excellent molecule for energy storage
-store twice as much energy as
carbohydrates
-animal fats are usually saturated fats and
are solid at room temperature
-plant fats (oils) are usually unsaturated and
are liquid at room temperature
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Lipids
Phospholipids -composed of:
-1 glycerol
-2 fatty acids
-a phosphate group

Phospholipids contain polar “heads”


(hydrohilic or water-loving) and nonpolar
“tails” (hydrophobic or water repelling).
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Lipids
Phospholipids spontaneously form micelles
or lipid bilayers in biological or living
cells.

These structures cluster the hydrophobic


regions of the phospholipid toward the
inside and leave the hydrophilic regions
exposed to the water environment.

Lipid bilayers are the basis of biological 40


membranes.

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