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    W3D - Proteins

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    W3D - Proteins

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    W3D - Proteins

    Uploaded by

    kakerusuzuki2007

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    of 2

    GENERAL

    BIOLOGY 1
    A.Y. 2022-2023

    Ateneo de Manila Senior High School


    Mardocheo Yao Crispino
    [email protected]

    PROTEINS
    Proteins: The Molecular Tools of the Cell
    Polypeptide chains - polymers of amino acids that are arranged in a specific linear sequence and are linked by
    peptide bonds.
    Protein – a macromolecule that consists of one or more polypeptide chains folded and coiled into specific
    conformations. They are abundant, making up 50% or more of cellular dry weight. They vary extensively in
    structure. The variation in structure results to varied function. They have important and varied functions in the
    cell:
    1. Structural support
    2. Storage (of amino acids)
    3. Transport (e.g., hemoglobin)
    4. Signaling (chemical messengers)
    5. Cellular response to chemical stimuli (receptor proteins)
    6. Movement (contractile proteins)
    7. Defense against foreign substances and disease-causing organisms (antibodies)
    8. Catalysis of biochemical reactions (enzymes)

    A. A polypeptide is a polymer of amino acids connected in a specific sequence


    Amino acid - building block molecule of a protein; most consist of an asymmetric carbon, termed the
    alpha carbon, which is covalently bonded to a(n): (1) hydrogen atom, (2) carboxyl group, (3) amino
    group, and (4) variable R group, which is specific to an amino acid. Physical and chemical properties of
    the side chain determine the uniqueness of each amino acid.

    Polypeptide chains are polymers that are formed when amino acid monomers are linked by peptide
    bonds.

    Peptide bond - covalent bond formed by a condensation reaction that links the carboxyl group of one
    amino acid to the amino group of another. Polypeptide chains range in length from a few monomers to
    more than a thousand.
    B. A protein’s function depends on its specific conformation
    The correlation between form and function in proteins is an emergent property resulting from
    superimposed levels of protein structures: (1) primary structure, (2) secondary structure, (3) tertiary
    structure, and (4) quaternary

    1. Primary structure
    Primary structure - unique sequence of amino acids in a protein. This is determined by genes. Slight
    change can affect a protein’s conformation and function (e.g., sickle-cell hemoglobin).

    2. Secondary structure
    Secondary structure - regular, repeated coiling and folding of a protein’s polypeptide backbone. It
    contributes to a protein’s overall conformation. It is stabilized by hydrogen bonds between peptide
    linkages in the protein’s backbone (carbonyl and amino groups).

    Alpha () helix - Secondary structure of a polypeptide that is a helical coil stabilized by hydrogen
    bonding between every fourth peptide bond. They are found in fibrous proteins (e.g., a-keratin and
    collagen) for most of their length and in some portions of globular proteins.

    Beta () pleated sheet - secondary protein structure which is a sheet of antiparallel chains folded
    into accordion pleats. Parallel regions are held together by either intrachain or interchain hydrogen
    bonds (between adjacent polypeptides).

    3. Tertiary structure
    Tertiary structure is the three-dimensional shape of a protein. The irregular contortions of a protein are
    due to bonding between and among side chains (R groups) and to interaction between R groups and the
    aqueous environment.

    4. Quaternary structure
    Quaternary structure - structure that results from the interactions between and among several
    polypeptides chains (subunits). Example: Collagen, a fibrous protein with three helical polypeptides
    supercoiled into a triple helix; found in animal connective tissue, collagen’s supercoiled quaternary
    structure gives it strength. Some globular proteins have subunits that fit tightly together. Example:
    Hemoglobin, a globular protein that has four subunits (two a chains and two b chains)

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