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    Protein Denaturation

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    Subir Das
    Protein denaturation involves the transformation of a protein's well-defined folded structure under physiological conditions into an unfolded state under non-physiological conditions. It occurs suddenly over a narrow range of conditions and is slowly reversible. Denaturation disrupts the balance of forces that stabilize the native structure, including hydrophobic interactions, hydrogen bonds, and electrostatic interactions. Increased temperature favors chain entropy and the unfolded state by disrupting these interactions, while solvent entropy opposes denaturation by hydrating the peptide chain. Denaturation results in loss of enzymatic activity and changes in texture, solubility, and potential toxicity.

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    Protein Denaturation

    Uploaded by

    Subir Das
    623 views17 pages
    Protein denaturation involves the transformation of a protein's well-defined folded structure under physiological conditions into an unfolded state under non-physiological conditions. It occurs suddenly over a narrow range of conditions and is slowly reversible. Denaturation disrupts the balance of forces that stabilize the native structure, including hydrophobic interactions, hydrogen bonds, and electrostatic interactions. Increased temperature favors chain entropy and the unfolded state by disrupting these interactions, while solvent entropy opposes denaturation by hydrating the peptide chain. Denaturation results in loss of enzymatic activity and changes in texture, solubility, and potential toxicity.

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    Protein Denaturation

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    Protein denaturation involves the transformation of a protein's well-defined folded structure under physiological conditions into an unfolded state under non-physiological conditions. It occurs suddenly over a narrow range of conditions and is slowly reversible. Denaturation disrupts the balance of forces that stabilize the native structure, including hydrophobic interactions, hydrogen bonds, and electrostatic interactions. Increased temperature favors chain entropy and the unfolded state by disrupting these interactions, while solvent entropy opposes denaturation by hydrating the peptide chain. Denaturation results in loss of enzymatic activity and changes in texture, solubility, and potential toxicity.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    623 views17 pages

    Protein Denaturation

    Uploaded by

    Subir Das
    Protein denaturation involves the transformation of a protein's well-defined folded structure under physiological conditions into an unfolded state under non-physiological conditions. It occurs suddenly over a narrow range of conditions and is slowly reversible. Denaturation disrupts the balance of forces that stabilize the native structure, including hydrophobic interactions, hydrogen bonds, and electrostatic interactions. Increased temperature favors chain entropy and the unfolded state by disrupting these interactions, while solvent entropy opposes denaturation by hydrating the peptide chain. Denaturation results in loss of enzymatic activity and changes in texture, solubility, and potential toxicity.

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    Protein Denaturation

    FDSC400

    Goals
    Denaturation Balance of forces Consequences of denaturation

    Effect of Temperature on Rate of Enzyme Action

    rate

    denaturant

    Denaturation
    Denaturation is a phenomenon that involves transformation of a well-defined, folded structure of a protein, formed under physiological conditions, to an unfolded state under non-physiological conditions.
    Occurs suddenly and completely over a narrow range of conditions Slowly reversible (if at all)

    Hydrophobic Interactions
    Clathrate water
    Increased solvent entropy Increased chain entropy

    Peptide chain

    Chain Entropy
    One native state

    S=k ln W

    Increased chain entropy

    Many denatured states

    Other Factors
    Hydrogen bonds Electrostatic interactions
    Consider how the total number and strength of these bonds changes as a result of denaturation

    Balance of Forces
    Chain entropy DG=DH-TDS

    Solvent entropy DG=DH-TDS

    other forces

    Effect of T on Balance of Forces


    Free energy change for denaturation

    Solvent entropy effect

    + (oppose)

    - (favor)

    Chain entropy effect

    Thermal Denaturation
    Trypsinogen 55C Pepsinogen 60C Lysozyme 72C Myoglobin 79C Soy Glycinin 92C Oat globulin 108C

    Affected by pH, water, solutes

    Table 11

    Why is Denaturation Sudden?


    100% Native Structure
    COOPERATIVE PROCESS Partly denatured structure is weaker so begins to change faster

    0% Critical value

    Concentration of denaturant or temperature

    Types of Denaturation
    Temperature Organic solvents Surface pH Shear

    Reversibility?
    One native form

    Refolding is a complex process particularly for large proteins or complex proteins

    Many denatured forms

    Energy Surface

    Free energy

    Many secondary minima amongst denatured states

    One native state (true energy minimum)

    Changes in Conformation

    Behavior of Denatured Protein


    Hydrophobic core Hydrophilic surface

    DENATURED
    Fast under non-physiological conditions

    Slow under physiological conditions

    NATIVE

    Unfolding forces some hydrophobic AA to surf

    AGGREGATED or other ingredient interactions

    Consequences of Denaturation
    Loss of enzymatic activity (death) Destruction of toxins Improved digestibility Loss of solubility Changes in texture

    Denaturation
    The conversion of a biologically functional molecule into a non-functional form There are many denatured states but one native state Proteins can regenerate to their native state but slowly Denatured proteins have a greater tendency to aggregate.

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