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    Biomolecules ??

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    resmaahresh

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    Biomolecules ??

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    resmaahresh
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    biomolecules ??

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    Biomolecules ??

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    resmaahresh

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    of 7

    Points to Remember

    Biomolecules : All the carbon compounds that we get from living tissues.
    Biomicromolecules : Molecules which have molecular weights less than
    one thousand dalton. They are also known as monomers.
    Biomacromolecules : Have molecular weight more than 10000 daltons
    generally 10,000 deltons and above. They are generally polymers.

    Primary and secondary metabolites :


     Primary metabolites have identifiable functions and play important roles in
    normal physiological process eg. Amino acids, nitrogenous bases, proteins
    and nucleic acid.
     Secondary metabolites are product of certain metabolic pathways from
    primary metabolites, eg. carotenoids, drugs, alkaloids, essential oils, rubber,
    gum, cellulose and resins etc.
    Amino acids : Organic compounds containing an amino group and one
    carboxyl group (acid group) and both these groups are attached to the same
    carbon atom called  carbon and so they are called amino acids.

    e.g. (1) In Glycine R = H


    (2) In alaine R = CH3
    (3) In serine R = CH2 – OH
     Twenty types of amino acids.
    Amino acid exists in Zwitterionic form at different pHs.
    R R R
    | | |

    (A) (B) (C)


    (Zwitterionic form)
     Based on number of amino and carboxyl groups, amino acids can be :
    (i) Aromatic–Tryptophan, phenylalanine and Tyrosine are aromatic (give
    smell) amino acids.
    Amino Acids

    Polar

    Acidic Basic Neutral


    e.g. aspartic acid e.g., Arginine e.g. valine, Proline
    glutamic acid
    (ii) Non Polar—Glutamine, tyrosine, serine

    Lipids :
     Water insoluble, containing C, H, O.
     Fats on hydrolysis yield fatty acids.
     Fatty acid has a carboxyl group attached to an R group (contains 1 to 19
    carbons).
     Fatty Acids : Saturated : With single bonds in carbon chain, e.g., Palmitic
    acid, butyric acid.
    Unsaturated : With one or more double bonds, e.g., oleic acid, linoleic acid.
     Glycerol : A simple lipid, is trihydroxy propane.

     Some lipid have fatty acids esterified with glycerol.


    Example of fatty acid (Palmitic acid) (CH3—(CH2)14—COOH)
     They can be monoglycerides, diglycerides and triglycerides.

    3
    Triglyceride (R1, R2, R3 are alkye groups in fatty acids.)
    Phospholipids (Lecithin) found in cell membrane and lipids made complex
    structure in neural tissue.
     Phospholipids are compound lipids with phosphorus and a phosphorylated
    organic compound e.g., Lecithin.
    Nitrogen bases
    (Carbon compounds with heterocyclic rings)

    Purine : Adenine, Guanine, Pyrimidine : Cytosine, Uracil, Thymine.


    Lipids are not strictly macromolecules as their molecular weight do not
    exceed 800 Da but form a part of the acid insoluble pool.
    Biomacromolecules : Biomolecules a with molecular weights in the
    range of ten thousand daltons and above; found in acid insoluble fraction. e.g.
    polysaccharides, nucleic acids, proteins and lipids.
    Nucleic acids : Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).
    Nucleoside : Nitrogenous base + Sugar e.g. Adenosine, guanosine.
    Nucleotide : Nitrogenous base + Sugar + Phosphate group. e.g. Adenylic
    acid, Guanylic acid. Thymidylic acid.
    DNA structure (Watson and Crick Model) : DNA is a right handed, double
    helix of two polynucleotide chains, having a major and minor groove. The two
    chains are antiparallel, and held together by hydrogen bonds (two between A
    and T and three between C and G). The backbone is formed by sugar-phosphate-
    sugar chain. The nitrogen bases are projected more or less perpendicular to this,
    backbone and face inside. The pitch is 34A°. At each step of ascent, the strand
    turns 36°. The rise per base pair is 3.4°A, so one full turn involves ten base pairs.
    Protein : proteins are polypeptides.
     They are polymers of aminoacids linked by peptide bond.

     Is a heteropolymer (different monomers repeating ‘n’ number of times).

     For functions of proteins refer Table 9.5, Page no. 147 NCERT, Text Book

    of Biology for Class XI.


    Structure of Proteins
    (a) Primary structure : Is found in the form of linear sequence of amino acids.
    First amino acid is called N-terminal amino acid and last amino acid is called
    C-terminal amino acid.
    (b) Secondary structure : Polypeptide chain undergoes folding or coiling which
    is stabilized-by hydrogen bonding. Right handed helices are observed; e.g.,
    fibrous protein in hair, nails.
    (c) Tertiary structure : Long protein chain is folded upon itself like a hollow
    woollen ball. Gives a 3-dimensional view of protein, e.g., myosin.
    (d) Quaternary structure : Two or more polypeptides with their foldings and
    coilings are arranged with respect to each other, e.g., Human haemoglobin
    molecule has 4 peptide chains - 2  and 2  submits.
    Monosaccharides are joined by glycosidic acid bond, right end is reducing
    and left end is non reducing
    Polysaccharides : Are long chain of polymers of monosaccharides.
    (a) Starch : Store house of energy in plant tissues. Forms helical secondary
    structures, made of only glucose monomers.
    (b) Cellulose : Homopolymer of glucose. It does not certain complex helices.
    Cotton fibre is cellulose.
    (c) Glycogen : Is a branched homopolymer, found as storage polysaccharide in
    animals.
    (d) Inulin : Is a polymer of fructose.
    (e) Chitin : Chemically modified sugar (amino-sugars) N-acetyl galactosamine
    form exoskeleton of arthropods; heterpolymer.
    Metabolic Pathways :
    (a) Anabolic pathways : Lead to formation of more complex structure from a
    simpler structure with the consumption of energy, e.g., Protein from amino
    acids., also known as biosynthetic pathways.
    (b) Catabolic pathway : Lead to formation of simpler structure from a complex
    structure, e.g., Glucose  Lactic Acid + energy
    The most important energy currency in living systems is ATP (adenosine
    tri – phosphate).
    “There is no uncatalysed metabolic conversion in living system”
    The living state is a non-equilibrium steady state to be able to perform work.
    Without metabolism, there cannot be a living state.
    Bonds linking monomers in a polymer
    Peptide bond—formed between the carboxyl (–COOH) group of one amino
    acid, and the amino (– NH2) group of the next amino with the elimination of water
    moiety, (dehydration).
    Glycosidic bond—bond formed between two carbon atoms of two adjacent
    monosaccharides., by dehydration.
    Phosphodiester bond—bond formed in nucleic acids where in a phosphate
    moiety links the 3-carbon of one sugar of one nucleotide to the 5-carbon of the
    sugar of the succeeding nucleotide. (The bond between phosphate group and
    hydroxyl group of sugar)
    Ezymes : Are biocatalyst.
     Almost all enzymes are proteins.

     Ribozymes–Nucleic acid that behave like enzymes.

     Has primary, secondary and tertiary structure.

     Active site of an enzyme is a crevice or pocket into which substrate fits.

     Enzymes get damaged at high temperatures.

     Enzymes isolated from thermophilic organisms (live under high temperatures)

    are thermostable.
     Enzymes accelerate the reactions many folds.

     Enzymes lower the activation energy of reactions. (Fig. 9.6, Page no. 156,

    NCERT Text Book of Biology for Class XI).


     E + S == ES  EP  E + P

    where E = Ezymes, S = Substrate, P = Product

    Factors affecting enzyme activity :


    (a) Temperature : Show highest activity at optimum temperature. Activity
    declines above and below the optimum value.
    (b) pH : Enzymes function in a narrow range of pH. Highest activity at optimum
    pH. (Fig. 9.7, Page no. 157, NCERT, Text Book of Biology for Class XI).
    (c) Concentration of substrate : The velocity of enzymatic reaction rises with
    increases in substrate concentration till it reaches maximum velocity (Vmax).
    Further increase of substrate does not increase the rate of reaction as no free
    enzyme molecules are available to bind with additional substrate.
    Enzyme inhibition : When the binding of a chemical shuts off enzyme
    activity, the process is called inhibition and chemical is called inhibitor.

    Competitive inhibition : Inhibitor closely resembles the substrate in its


    molecular structure and inhibits the enzyme activity. E.g., inhibition of succinic
    dehydrogenase by malonate. (Actual is succinic acid).

    Classification of enzymes :
    1. Oxidoreductase/dehydrogenases : Catalyse oxidoreduction between 2
    substrates. S reduced + S oxidised  S oxidised + S reduced.

    2. Transferases : Catalyse transfer of a group between a pair of substrates.

    S – G + S  S + S – G

    3. Hydrolases : Catalyse hydrolysis of ester, ether, peptide, glycosidic, C–C,


    P-N bonds.

    4. Lyases : Catalyse removal of groups from substrates by mechanisms other


    than hydrolysis. Leave double bonds.

    5. Isomerases : Catalyse inter-conversion of optical, geometrical or positional


    isomers.

    6. Ligases : Catalyse linking together of 2 compounds.

    C–O, C–S, C–N, P–O

    Co-factors : Enzymes becomes catalytically become active when it binds


    to non protein constituent called co-factors. Protein portion of enzyme is
    called apoenzyme.
     Prosthetic group : These are organic compound which tightly bound to the
    apoenzyme.

    e. g., Haem is prosthetic group in peroxidase and catalase.


     Coenzyme : These are organic compounds whose association with the
    apoenzyme is only transient, usually occurring during the course of catalysis.

    e.g., Coenzyme Nicotinamide adenine dinucleotide (NAD) and NADP


    contain vitamin niacin.

     Metal ions : Metal ions form coordination bond with side chains at the
    active site and at the same time form one or more coordination bond with
    substrate.

    e.g. zinc in enzyme carboxy peptidase.

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