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    Protein Structure

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    gamer sonjoy
    In this ppt we will ex

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    © All Rights Reserved
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    Protein Structure

    Uploaded by

    gamer sonjoy
    19 views12 pages
    In this ppt we will ex

    Original Title

    Protein structure

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    © © All Rights Reserved

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    In this ppt we will ex

    Copyright:

    © All Rights Reserved
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    Download as pptx, pdf, or txt
    19 views12 pages

    Protein Structure

    Uploaded by

    gamer sonjoy
    In this ppt we will ex

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    of 12

     Different structure of protein

     Conformational change of protein

    Presented by
    Sonjoy paul
    Roll:35
    Dhaka International University
    Protein structure

    Title text addition


    Protein structure
    Primary Structure:
    This is the linear sequence of amino acids in a polypeptide chain.
    Each amino acid is linked to the next by peptide bonds, forming a
    backbone. The sequence is dictated by the genetic code encoded in
    DNA.

    Title text addition

    Secondary Structure: This refers to the local folding


    patterns of the polypeptide chain, mainly stabilized by
    hydrogen bonds. Common secondary structures include alpha
    helices and beta sheets.
    Protein structure
    The alpha helix is a right-hand - helix
    conformation which is a very common
    structural arrangement in the secondary
    structure of proteins.

    Title text addition


    Formation
    In it, every backbone N−H group hydrogen bonds
    to the backbone C=O group of the amino acid that
    is four residues earlier in the protein sequence.
    Protein structure

    Beta Sheet:Structure: It's another common


    secondary structure in proteins, consisting of
    multiple polypeptide strands lying alongside each
    other.

    Title text addition

    Formation: The strands are connected by hydrogen


    bonds between the carbonyl oxygen of one strand
    and the amide hydrogen of an adjacent strand,
    forming either parallel or antiparallel arrangements.
    Protein structure

    Title text addition


    Protein structure

    Tertiary Structure: This is the overall three-


    dimensional shape of a single polypeptide
    chain, resulting from interactions between
    amino acid side chains (e.g., hydrophobic
    interactions, hydrogen bonds, disulfide bonds).
    Title text addition
    Protein structure

    Quaternary Structure: Quaternary structure refers to the


    arrangement of multiple polypeptide chains (subunits) in a
    protein complex. The individual subunits may have their own
    tertiary structures, and the overall quaternary structure is
    stabilized by interactions similar to those in tertiary structure,
    such as hydrogen bonds, hydrophobic interactions, and disulfide
    Title text addition
    bonds.

    Quaternary structure is essential for the function of many


    proteins, particularly those with multiple subunits, such as
    enzymes and hemoglobin.
    Conformational changes in proteins

    Proteins are dynamic molecules that can adopt different conformations, or shapes,
    depending on their environment and interactions. Conformational changes are
    essential for proteins to carry out their functions effectively.

    Conformational Changes
    Title text addition
    Ligand Binding: When a protein binds to a ligand (such as a substrate,
    hormone, or inhibitor), it often undergoes conformational changes. These
    changes can involve small adjustments in the positions of amino acids or
    larger-scale movements of protein domains.
    Conformational changes in proteins

    Allosteric Regulation: Some proteins have allosteric sites separate from their active sites.
    Binding of a molecule to these allosteric sites can induce conformational changes that affect the
    protein's activity at the active site.
    Temperature and pH: Changes in temperature or pH can alter the stability and conformation
    of proteins. High temperatures or extreme pH levels can denature proteins, causing them to
    unfold and lose their function.
    Post-translational Modifications: Proteins can undergo post-translational modifications
    such as phosphorylation, or acetylation, which can induce conformational changes. These
    modifications can affect protein-protein interactions, enzyme activity, and cellular signaling
    pathways.
    Protein Folding: Newly synthesized proteins often need to fold into their correct three-
    dimensional structures to become functional. This process involves conformational changes as
    the protein chain rearranges itself to achieve the lowest energy state.
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