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    Quaternary Structure of Proteins

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    마스러버
    This document discusses quaternary protein structures, which are composed of multiple polypeptide chains or subunits. Various interactions hold the subunits together, including ionic bonds, van der Waals forces, hydrogen bonds, and hydrophobic interactions. Disulfide bonds also play a role. Some proteins contain non-peptide prosthetic groups that are important for function, such as the heme group in hemoglobin and myoglobin. Fibrous proteins have structural roles while globular proteins serve as transporters, regulators, and enzymes.

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    Quaternary Structure of Proteins

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    마스러버
    26 views18 pages
    This document discusses quaternary protein structures, which are composed of multiple polypeptide chains or subunits. Various interactions hold the subunits together, including ionic bonds, van der Waals forces, hydrogen bonds, and hydrophobic interactions. Disulfide bonds also play a role. Some proteins contain non-peptide prosthetic groups that are important for function, such as the heme group in hemoglobin and myoglobin. Fibrous proteins have structural roles while globular proteins serve as transporters, regulators, and enzymes.

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    This document discusses quaternary protein structures, which are composed of multiple polypeptide chains or subunits. Various interactions hold the subunits together, including ionic bonds, van der Waals forces, hydrogen bonds, and hydrophobic interactions. Disulfide bonds also play a role. Some proteins contain non-peptide prosthetic groups that are important for function, such as the heme group in hemoglobin and myoglobin. Fibrous proteins have structural roles while globular proteins serve as transporters, regulators, and enzymes.

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    26 views18 pages

    Quaternary Structure of Proteins

    Uploaded by

    마스러버
    This document discusses quaternary protein structures, which are composed of multiple polypeptide chains or subunits. Various interactions hold the subunits together, including ionic bonds, van der Waals forces, hydrogen bonds, and hydrophobic interactions. Disulfide bonds also play a role. Some proteins contain non-peptide prosthetic groups that are important for function, such as the heme group in hemoglobin and myoglobin. Fibrous proteins have structural roles while globular proteins serve as transporters, regulators, and enzymes.

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    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    of 18

    QUATERNAR

    Y EJORANGO,
    ESTOCONING,
    STRUCTURES PARDILLO, PINILI

    IN PROTEIN
    QUATERNARY
    STRUCTURES
    SOME PROTEINS ARE
    MADE UP OF MULTIPLE
    POLYPEPTIDE CHAINS,
    ALSO KNOWN AS SUBUNITS
    WHAT HOLDS
    THEM TOGETHER?

     IN GENERAL, THE SAME


    TYPES OF INTERACTIONS
    THAT CONTRIBUTE TO
    TERTIARY STRUCTURE
    ALSO HOLD THE
    SUBUNITS TOGETHER TO
    GIVE QUATERNARY
    STRUCTURE.
    IONIC BONDS
     SOME AMINO ACIDS HAVE A
    CHARGED SIDE-CHAIN,
    WHICH IS EITHER
    NEGATIVE OR POSITIVE.
    NEGATIVELY CHARGED
    SIDE-CHAINS ARE
    ATTRACTED TO POSITIVELY
    CHARGED SIDE-CHAINS,
    WHILE BEING REPELLED BY
    ANOTHER NEGATIVELY
    CHARGED SIDE-CHAINS.
    WHEN TWO OPPOSITE
    CHARGED CHAINS COME
    TOGETHER, THEY FORM
    WHAT IS CALLED A “SALT
    BRIDGE”.
    VAN DER WAALS FORCE

     VAN DER WAALS FORCES ARE ALSO


    SIMILAR TO ELECTROSTATIC BONDS. THE  ATTRACTIONS CAN OCCUR BETWEEN ANY
    FORMATION OF VAN DER WAALS FORCES TWO OR MORE MOLECULES AND ARE
    DEPENDS ON THE SHAPE OF THE SIDE- DEPENDENT ON SLIGHT FLUCTUATIONS OF
    CHAIN; IF THE ATOMS WITHIN THE SIDE- THE ELECTRON DENSITIES, WHICH ARE
    CHAINS OF NEIGHBORING AMINO ACIDS NOT ALWAYS SYMMETRICAL AROUND AN
    FIT WELL, THEN VAN DER WAALS FORCE IS ATOM.
    FORMED.
    VAN DER WAALS FORCE
     WHEN AN OH GROUP COMES ACROSS ANOTHER ATOM WITH
    A SLIGHTLY NEGATIVE CHARGE, SUCH AS OXYGEN, THE
    HYDROGEN FROM THE OH GROUP REACHES OUT TO THE
    HYDROGEN BONDS OXYGEN ATOM AND FORMS A BOND. THIS IS KNOWN AS A
    HYDROGEN BOND AND OCCURS BETWEEN AMINO ACIDS
    WHICH HAVE WHAT IS CALLED A POLAR SIDE-CHAIN.
    DISULFIDE BONDS
     DISULFIDE BONDS ARE
    FORMED BETWEEN TWO
    SULFUR (SH) ATOMS,
    WHICH ARE FOUND IN
    THE SIDE-CHAIN OF THE
    AMINO ACID CYSTEINE.
    WHEN TWO CYSTEINES
    ARE BROUGHT INTO
    CLOSE PROXIMITY IN
    THE TERTIARY
    STRUCTURE, AN ENZYME
    CALLED “PROTEIN
    DISULFIDE ISOMERASE”
    FORMS A DISULFIDE
    BOND BETWEEN THE
    TWO SH GROUPS.
    HYDROPHOBIC
    INTERACTIONS
     SOME AMINO ACIDS HAVE
    SIDE-CHAINS WHICH REPEL
    WATER. THESE AMINO
    ACIDS WITH HYDROPHOBIC
    SIDE-CHAINS ARE OFTEN
    FOUND ON THE INSIDE OF
    PROTEINS, AND DUE TO THE
    HYDROPHOBIC NATURE OF
    THESE AMINO ACIDS THEY
    INTERACT WITH ONE
    ANOTHER BY WHAT IS
    CALLED HYDROPHOBIC
    “INTERACTIONS”.
    STRUCTURES & FUNCTION

    FIBROUS STRUCTURE GLOBULAR STRUCTURE

     HAS A STRONG MECHANICAL STRENGTH  SERVE AS TRANSPORT PROTEINS,

     USUALLY MAKES UP MAJOR COMPONENTS REGULATORY PROTEINS, AND ENZYMES


    OF CELLS  SPHERICAL IN SHAPE

     ELONGATED AND STRAND-LIKE  E.G. HEMOGLOBIN, MYOGLOBIN

     E.G. KERATIN, COLLAGEN


    FIBROUS VS GLOBULAR
    CONJUGATED
    PROTEINS
    • NON-PROTEIN GROUPS
    CALLED PROSTHETIC
    GROUPS MAY ALSO BE
    ASSOCIATED WITH
    POLYPEPTIDE CHAINS
    • POLYPEPTIDE CHAIN +
    PROSTHETIC GROUP =
    CONJUGATED PROTEIN
    HEME
    GROUP
     PROSTHETIC GROUP OF
    A PROTOPORPHYRIN
    RING AND A CENTRAL
    IRON ATOM
     THEY HAVE THE ABILITY
    TO REVERSIBLY BIND
    WITH OXYGEN DUE TO
    THEIR IRON
    HEMOGLOBIN
     FOUND IN RED BLOOD
    CELLS
     TRANSPORTS OXYGEN

     IT IS A TETRAMER I.E IT
    HAS 4 SUBUNITS: 2
    ALPHA, 2 BETA
     EACH SUBUNIT HAS A
    HEME GROUP
    MYOGLOBIN
     FOUND IN SKELETAL
    MUSCLE
     OXYGEN STORAGE

     MONOMER

     HAS GREATER ATTRACTION


    FOR OXYGEN THAN
    HEMOGLOBIN WHICH
    ALLOWS EFFICIENT
    TRANSFER OF OXYGEN
    FROM BLOODSTREAM TO
    BODY CELLS
    SOURCES

     Denniston, K., Topping, J., & Dorr, Q. D. (2016). General, Organic, and Biochemistry [E-book]. In General, Organic,
    and Biochemistry (9th ed., p. 646). McGraw-Hill Education.
     Yokoyama, M., PhD. (2019, January 25). Intermolecular Forces in Tertiary Protein Structure. News-Medical.Net.
    https://www.news-medical.net/life-sciences/Intermolecular-Forces-in-Tertiary-Protein-Structure.aspx

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