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    1.4 Proteins

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    BlitzSZN
    This document discusses several key factors that influence enzyme-substrate interactions and enzyme reaction rates. It notes that the three-dimensional shape of the enzyme's active site is complementary to that of the substrate. It also lists several factors that can affect the rate of enzyme reactions, including temperature, pH, substrate and enzyme concentrations, and the presence of inhibitors. Finally, it provides context on protein structure and folding, noting how the primary structure of amino acids determines the overall three-dimensional structure of the protein.

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    1.4 Proteins

    Uploaded by

    BlitzSZN
    11 views1 page
    This document discusses several key factors that influence enzyme-substrate interactions and enzyme reaction rates. It notes that the three-dimensional shape of the enzyme's active site is complementary to that of the substrate. It also lists several factors that can affect the rate of enzyme reactions, including temperature, pH, substrate and enzyme concentrations, and the presence of inhibitors. Finally, it provides context on protein structure and folding, noting how the primary structure of amino acids determines the overall three-dimensional structure of the protein.

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    This document discusses several key factors that influence enzyme-substrate interactions and enzyme reaction rates. It notes that the three-dimensional shape of the enzyme's active site is complementary to that of the substrate. It also lists several factors that can affect the rate of enzyme reactions, including temperature, pH, substrate and enzyme concentrations, and the presence of inhibitors. Finally, it provides context on protein structure and folding, noting how the primary structure of amino acids determines the overall three-dimensional structure of the protein.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Flag for inappropriate content
    Download as pdf or txt
    11 views1 page

    1.4 Proteins

    Uploaded by

    BlitzSZN
    This document discusses several key factors that influence enzyme-substrate interactions and enzyme reaction rates. It notes that the three-dimensional shape of the enzyme's active site is complementary to that of the substrate. It also lists several factors that can affect the rate of enzyme reactions, including temperature, pH, substrate and enzyme concentrations, and the presence of inhibitors. Finally, it provides context on protein structure and folding, noting how the primary structure of amino acids determines the overall three-dimensional structure of the protein.

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    © All Rights Reserved
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    of 1

    Enzyme and Substrate shape is Contains peptide

    substrate complementary to Active site bonds


    Temperature active site
    concentrations
    Factors Induced-
    fit model Specific Sequence of AAs in
    Competitive and
    affecting Enzyme- structure of primary structure
    non-competitive enzyme substrate active site Polypeptide determines where
    inhibitors reactions complexes chain bonds form, and
    Structure hence 3D structure
    Lower activation of protein
    determines Primary
    pH energy of the Enzymes
    reaction function structure
    Biological
    Purple = positive catalysts Folding ɑ-helix or β-
    result sheet

    Biuret 1.4 PROTEINS Structure


    Secondary
    structure
    Blue = negative
    reagent Test Hydrogen bonds
    result and folding between NH
    and CO groups
    NH2 group, COOH group, R Quaternary
    side chain and H bond all Amino acid (AA) structure Tertiary
    attached to central Monomers structure Specific 3D
    carbon atom shape of protein
    Dipeptide - 2 AAs Protein can Contains ionic bonds,
    20 AAs occur in living contain multiple disulfide bridges and
    organisms, differ only Polypeptide - many AAs polypeptides
    Multiple polypeptide hydrogen bonds
    in the R side chain
    chains linked together
    Condensation reaction
    Peptide bonds AQA
    https://bit.ly/pmt-cc
    https://bit.ly/pmt-edu https://bit.ly/pmt-cc

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