Scribd Logo
Upload

Welcome to Scribd!

  • 130 views

    Proteins

    Uploaded by

    api-260674021
    Proteins are the most structurally and functionally diverse molecules in biology. They are involved in almost all cellular functions through roles as enzymes, structural components, carriers, transporters, cell signaling molecules, receptors, antibodies, and more. Proteins are polymers of amino acids linked by peptide bonds. The 20 different amino acids vary in properties based on their variable R groups. Protein structure is hierarchical, progressing from primary structure of the amino acid sequence to complex three-dimensional tertiary and quaternary structures essential for protein function. Protein shape and interactions between amino acids are determined by forces like hydrogen bonds, hydrophobic interactions, and disulfide bridges.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Flag for inappropriate content

    You might also like

    Proteins

    Uploaded by

    api-260674021
    130 views25 pages
    Proteins are the most structurally and functionally diverse molecules in biology. They are involved in almost all cellular functions through roles as enzymes, structural components, carriers, transporters, cell signaling molecules, receptors, antibodies, and more. Proteins are polymers of amino acids linked by peptide bonds. The 20 different amino acids vary in properties based on their variable R groups. Protein structure is hierarchical, progressing from primary structure of the amino acid sequence to complex three-dimensional tertiary and quaternary structures essential for protein function. Protein shape and interactions between amino acids are determined by forces like hydrogen bonds, hydrophobic interactions, and disulfide bridges.

    Original Description:

    Original Title

    proteins

    Copyright

    © © All Rights Reserved

    Available Formats

    PPT, PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Report this Document
    Proteins are the most structurally and functionally diverse molecules in biology. They are involved in almost all cellular functions through roles as enzymes, structural components, carriers, transporters, cell signaling molecules, receptors, antibodies, and more. Proteins are polymers of amino acids linked by peptide bonds. The 20 different amino acids vary in properties based on their variable R groups. Protein structure is hierarchical, progressing from primary structure of the amino acid sequence to complex three-dimensional tertiary and quaternary structures essential for protein function. Protein shape and interactions between amino acids are determined by forces like hydrogen bonds, hydrophobic interactions, and disulfide bridges.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Flag for inappropriate content
    Download as ppt, pdf, or txt
    130 views25 pages

    Proteins

    Uploaded by

    api-260674021
    Proteins are the most structurally and functionally diverse molecules in biology. They are involved in almost all cellular functions through roles as enzymes, structural components, carriers, transporters, cell signaling molecules, receptors, antibodies, and more. Proteins are polymers of amino acids linked by peptide bonds. The 20 different amino acids vary in properties based on their variable R groups. Protein structure is hierarchical, progressing from primary structure of the amino acid sequence to complex three-dimensional tertiary and quaternary structures essential for protein function. Protein shape and interactions between amino acids are determined by forces like hydrogen bonds, hydrophobic interactions, and disulfide bridges.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Flag for inappropriate content
    Download as ppt, pdf, or txt
    of 25

    Proteins

    AP Biology

    Proteins
    Multipurpose
    molecules

    AP Biology

    2008-2009

    Proteins
    Most structurally & functionally diverse group
    Function: involved in almost everything

    AP Biology

    enzymes (pepsin, DNA polymerase)


    structure (keratin, collagen)
    carriers & transport (hemoglobin, aquaporin)
    cell communication
    signals (insulin & other hormones)
    receptors
    defense (antibodies)
    movement (actin & myosin)
    storage (bean seed proteins)

    Proteins
    Structure

    H2O

    monomer = amino acids


    20 different amino acids

    polymer = polypeptide
    protein can be one or more polypeptide

    chains folded & bonded together


    large & complex molecules
    complex 3-D shape
    hemoglobin

    AP Biology

    Rubisco

    growth
    hormones

    Amino acids
    Structure
    central carbon
    amino group
    carboxyl group (acid)
    R group (side chain)

    H O
    H
    | ||
    N
    C COH
    |
    H
    R

    variable group
    different for each amino acid
    confers unique chemical

    properties to each amino acid


    like 20 different letters of an
    AP Biology

    alphabet
    can make many words (proteins)

    Oh, I get it!


    amino = NH2
    acid = COOH

    Effect of different R groups:


    Nonpolar amino acids
    nonpolar & hydrophobic

    AP Biology

    Why are these nonpolar & hydrophobic?

    Effect of different R groups:


    Polar amino acids
    polar or charged & hydrophilic

    AP Biology

    Why are these polar & hydrophillic?

    Ionizing in cellular waters

    AP Biology

    H+ donors

    Ionizing in cellular waters

    AP Biology

    H+ acceptors

    Sulfur containing amino acids


    Form disulfide bridges

    covalent cross links betweens sulfhydryls


    stabilizes 3-D structure

    H-S S-H
    You wondered
    why perms
    smell like
    rotten eggs?

    AP Biology

    Building proteins
    Peptide bonds
    covalent bond between NH2 (amine) of
    one amino acid & COOH (carboxyl) of
    another
    CN bond

    H2O

    dehydration synthesis

    AP Biology

    peptide
    bond

    Building proteins
    Polypeptide chains have direction
    N-terminus = NH2 end
    C-terminus = COOH end
    repeated sequence (N-C-C) is the
    polypeptide backbone

    can only grow in one direction

    AP Biology

    Protein structure & function


    Function depends on structure

    3-D structure
    twisted, folded, coiled into unique shape

    pepsin

    hemoglobin
    AP Biology

    collagen

    Primary (1) structure


    Order of amino acids in chain
    amino acid sequence
    determined by gene (DNA)
    slight change in amino acid
    sequence can affect proteins
    structure & its function

    even just one amino acid change

    can make all the difference!

    AP Biology

    lysozyme: enzyme in
    tears & mucus that
    kills bacteria

    Sickle cell anemia

    AP Biology

    Im
    hydrophilic!

    Just 1
    out of 146
    amino acids!

    But Im
    hydrophobic!

    Secondary (2) structure


    Local folding
    folding along short sections of polypeptide
    interactions between
    adjacent amino acids

    H bonds
    weak bonds
    between R groups

    forms sections of
    3-D structure
    -helix
    -pleated sheet

    AP Biology

    Secondary (2) structure

    AP Biology

    Tertiary (3) structure


    Whole molecule folding

    interactions between distant amino acids


    hydrophobic interactions

    cytoplasm is
    water-based
    nonpolar amino
    acids cluster away
    from water
    H bonds & ionic bonds
    disulfide bridges
    covalent bonds between
    AP Biology

    sulfurs in sulfhydryls (SH)


    anchors 3-D shape

    Quaternary (4) structure


    More than one polypeptide chain bonded
    together

    only then does polypeptide become


    functional protein
    hydrophobic interactions

    AP Biology
    collagen
    = skin & tendons

    hemoglobin

    Protein structure (review)


    R groups
    hydrophobic interactions
    disulfide bridges
    (H & ionic bonds)

    amino acid
    sequence
    peptide bonds
    determined
    by DNA
    AP Biology

    4
    2
    R groups
    H bonds

    multiple
    polypeptides
    hydrophobic
    interactions

    Protein denaturation
    Unfolding a protein

    In Biology,
    size doesnt matter,
    SHAPE matters!

    conditions that disrupt H bonds, ionic


    bonds, disulfide bridges
    temperature
    pH
    salinity

    alter 2 & 3 structure


    alter 3-D shape

    destroys functionality
    some proteins can return to their functional shape

    after denaturation, many cannot


    AP Biology

    EAT

    Lets build
    X some

    Proteins!

    AP Biology

    2008-2009

    Ghosts of Lectures Past


    (storage)

    AP Biology

    2007-2008

    Chaperonin proteins
    Guide protein folding

    AP Biology

    provide shelter for folding polypeptides


    keep the new protein segregated from
    cytoplasmic influences

    Protein models
    Protein structure visualized by
    X-ray crystallography
    extrapolating from amino acid sequence
    computer modelling

    lysozyme
    AP Biology

    You might also like