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  • newPROTEIN LEC. 2 - DR. PRAFUL RAMTEKE

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    This document provides an overview of protein chemistry, including the chemical properties of amino acids, biologically important peptides, protein denaturation, and the primary, secondary, tertiary, and quaternary structures of proteins. It describes the reactions of amino acid functional groups, biologically important peptides like glutathione and hormones, how denaturation disrupts protein structure, and how proteins fold from their primary amino acid sequences into defined secondary and tertiary structures stabilized by hydrogen bonds and other weak interactions.

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    Protein chemistry -2

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    This document provides an overview of protein chemistry, including the chemical properties of amino acids, biologically important peptides, protein denaturation, and the primary, secondary, tertiary, and quaternary structures of proteins. It describes the reactions of amino acid functional groups, biologically important peptides like glutathione and hormones, how denaturation disrupts protein structure, and how proteins fold from their primary amino acid sequences into defined secondary and tertiary structures stabilized by hydrogen bonds and other weak interactions.

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    © All Rights Reserved
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    5 views29 pages

    newPROTEIN LEC. 2 - DR. PRAFUL RAMTEKE

    Uploaded by

    Aarohi
    This document provides an overview of protein chemistry, including the chemical properties of amino acids, biologically important peptides, protein denaturation, and the primary, secondary, tertiary, and quaternary structures of proteins. It describes the reactions of amino acid functional groups, biologically important peptides like glutathione and hormones, how denaturation disrupts protein structure, and how proteins fold from their primary amino acid sequences into defined secondary and tertiary structures stabilized by hydrogen bonds and other weak interactions.

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    © All Rights Reserved
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    of 29

    Protein chemistry

    LECTURE-02
    Learning Objectives

    ⚫ Chemical properties of amino acids


    ⚫ Biologically important peptides
    ⚫ Denaturation
    ⚫ Structure of protein.
    Primary structure
    Secondary structure
    Chemical properties of Amino acids

    ⚫Reactions due to –COOH group


    1. Amino acids form salts –COONa with bases and
    esters –COOR’ with alcohols;
    2. Decarboxylation :

    e..g. Histamine, tyramine & GABA

    3. Reaction with ammonia


    ⚫Reactions due to –NH2 Group
    1. Combines with acids to form salt –NH3+Cl-

    1. Reaction with Ninhydrin: forms Ruhemann’s


    purple (for quantitaive determination of amino
    acids and protein)
    3. Colour reactions of amino acids
    4. Transamination reactions

    5. Oxidative deamination: liberates free ammonia


    BIOLOGICALLY IMPORTANT
    PEPTIDES
    BIOLOGICALLY IMPORTANT PEPTIDES
    ⚫A.A Less than 10
    ⚫Glutathione: lt is a tripeptide composed of
    3 amino acids.
    Glutamyl-cysteinyl-glycine
    Glutathione
    2. Thyrotropin Releasing Hormone: tripeptide
    3. oxytocin: nonapeptide
    4. Vasopressin : nonapeptide
    5. Angiotensin I (10 AA), Angiotensin II (8 AA)
    6. Methionine enkephalin: pentapeptide
    7. Bradykinin (nonapeptide), kallidin (decapeptide)
    8. Peptide antibiotics: Gramicidin, Bacitracin,
    Actinomycin
    9. Aspartame: Dipeptide (artificial sweetner)
    10. GIT Hormones: Gastrin, secretin
    Denaturation of protein
    Levels of organizations of proteins

    Primary structure

    Secondary

    Tertiary

    Quaternary
    Primary structure
    ⚫ Number and Sequence of amino acids.
    ⚫ Covalently linked by peptide bonds or some time disulfide
    linkage.
    ⚫ Each amino acid is called a "residue” or “moiety”.
    ⚫ Starts from the amino terminal (N) end and ends in the
    carboxyl terminal (C) end.
    ⚫ Structure of Insulin- by Frederik Sanger
    Protein folding
    ⚫ The protein can fold and orient the R groups in favorable
    positions.
    ⚫ Weak non-covalent interactions will hold the protein in its
    functional shape
    ⚫ These are weak and will take
    many to hold the shape.
    Determination of primary structure of
    protein

    1. Determination of amino acid composition

    1. Degradation of protein or polypeptide into smaller


    fragments

    1. Determination of amino acid sequence


    Secondary structure
    ⚫ It is a local, regularly occurring structure in proteins and
    is mainly formed through hydrogen bonds between
    backbone atoms.
    ⚫ Pauling & Corey studied the secondary structures and
    proposed 2 conformations.
    1. α helix
    2. β sheets
    3. Turns, Bends, Loops
    Alpha helix
    ⚫ Most common. Right handed and spiral structure.

    ⚫ Stabilized by hydrogen bonds between NH and C=O groups.

    ⚫ Side chain extend outwards.

    ⚫ Amino acids per turn – 3.6

    ⚫ Ex. found in many globular proteins like Myoglobin,

    Haemoglobin
    Beta pleated sheet
    ⚫ 2 or more polypeptides line up side by side.
    ⚫ Stabilized by hydrogen bond between N-H and C=O groups of
    adjacent chains.
    ⚫ Ex. Carbonic unhydrase
    Thank you

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