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    4 - Protein Structure

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    Innocent Tebulo
    This document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. [1] Primary structure refers to the linear sequence of amino acids that make up a protein. [2] Secondary structure involves regular patterns of hydrogen bonds that form alpha helices and beta sheets. [3] Tertiary structure describes how secondary structure units fold into specific three-dimensional shapes. [4] Quaternary structure occurs when multiple protein subunits associate into complexes.

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    4 - Protein Structure

    Uploaded by

    Innocent Tebulo
    5 views30 pages
    This document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. [1] Primary structure refers to the linear sequence of amino acids that make up a protein. [2] Secondary structure involves regular patterns of hydrogen bonds that form alpha helices and beta sheets. [3] Tertiary structure describes how secondary structure units fold into specific three-dimensional shapes. [4] Quaternary structure occurs when multiple protein subunits associate into complexes.

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    4_Protein Structure

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    This document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. [1] Primary structure refers to the linear sequence of amino acids that make up a protein. [2] Secondary structure involves regular patterns of hydrogen bonds that form alpha helices and beta sheets. [3] Tertiary structure describes how secondary structure units fold into specific three-dimensional shapes. [4] Quaternary structure occurs when multiple protein subunits associate into complexes.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    5 views30 pages

    4 - Protein Structure

    Uploaded by

    Innocent Tebulo
    This document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. [1] Primary structure refers to the linear sequence of amino acids that make up a protein. [2] Secondary structure involves regular patterns of hydrogen bonds that form alpha helices and beta sheets. [3] Tertiary structure describes how secondary structure units fold into specific three-dimensional shapes. [4] Quaternary structure occurs when multiple protein subunits associate into complexes.

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    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    of 30

    Protein Structure

    Collins Edward Jana, PhD

    Biochemistry Division, Biomedical


    Sciences Department
    Learning outcomes
    References
    Peptides and Polypeptides
    Proteins are Polypeptides
    Proteins bury hydrophobic residues in
    their core
    Peptides and Polypeptides
    Levels of Protein Structure
    Levels of Protein Structure
    Primary Structure
    Primary Structure
    Protein Folding
    Molecular chaperones
    Degradation of misfolded protein
    2. Secondary Structure
    The  helix structure
    The helix structure
    The pleated sheets
    The pleated sheets
    The pleated sheets
    Anti-parallel -sheet

    Hydrogen bonds between NH & CO grps connect


    each amino acid to a single amino acid on
    adjacent strand, stabilizing the structure
    The pleated sheets
    Mixed -sheet
    The pleated sheets
    In the case of anti-parallel β-sheet, the polypeptide
    makes tight “β-turns” or “hair pin” bends to fold the
    chain back on itself.

    β-Turns and bends: short segments of AAs that join


    2 units of 2o structure
    β turn or β bend involves 4 aminoacyl residues, in
    which the first residue is H-bonded to the 4 th resulting
    in a 180° turn
    Proline & Glycine are often present in β turns
    β-turn or bends
    Connecting loops
    These are unstructured polypeptides that connect α-
    helices to β-sheets in a protein

    When illustrating a protein structure, an α-helix is


    represented either as a solid cylinder, or as a helical
    ribbon. While β-strands are represented as broad arrows
    3.Tertiary Structure
    Mixture of various 2o structures are folded up and
    packed together to form a compact structure (protein
    molecule).

    This is largely the result of interactions of the side


    chains of the amino acids, both with each other and
    with the environment.

    Staphylococcal nuclease
    Myoglobin
    4.Quaternary Structure
    Once a tertiary structure is formed, we now have a
    protein molecule, & for many proteins, that is the final
    Stage.

    Many functional proteins have more than one such


    protein molecule or protein monomer. These
    monomers link together by 2o bonds.

    The monomers may be the same or different, & the


    resulting multi-component molecules are variously
    called dimers, tetramers, or oligomers in which 2 or 4
    or more monomers have combined to form one
    functional protein
    Quaternary Structure
    Different terms are used to describe subunit
    structure. The prefixes “homo” or “hetero” are used to
    describe identical or different subunits respectively,
    of 2, 3, or 4 subunit proteins.

    Crop protein of bacteriophage

    dimer
    tetramer of human hemoglobin
    Forces stabilizing Protein Structure
    1.Hydrogen bonding:
    The hydrogen on one
    molecule attached to
    O or N that is attracted
    to an O or N of a different
    molecule

    2.Ionic interactions:
    -vely charged grps can interact
    with +vely charged grps
    Forces stabilizing Protein Structure

    3.Disulphide bonds:
    The –SH grps of 2 cysteine
    molecules in different regions
    of a protein can undergo an
    oxidation reaction to form a
    disulphide (-S-S-) bridge
    between the 2 chains
    Forces stabilizing Protein Structure
    4.Hydrophobic bonds:

    Hydrophobic amino acids


    associate with each other to
    form hydrophobic bonds

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