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    6 Proteins - Intro

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    emanuel coates
    Proteins are the most structurally and functionally diverse molecules in biology. They perform many important functions through their unique three-dimensional structures, which are determined by their sequences of amino acids. Proteins fold into complex shapes through interactions between amino acid side chains within their primary, secondary, tertiary, and sometimes quaternary structures. Changes in a protein's amino acid sequence or structure can significantly impact its function in the cell.

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    6 Proteins - Intro

    Uploaded by

    emanuel coates
    42 views25 pages
    Proteins are the most structurally and functionally diverse molecules in biology. They perform many important functions through their unique three-dimensional structures, which are determined by their sequences of amino acids. Proteins fold into complex shapes through interactions between amino acid side chains within their primary, secondary, tertiary, and sometimes quaternary structures. Changes in a protein's amino acid sequence or structure can significantly impact its function in the cell.

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    6 Proteins - intro

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    Proteins are the most structurally and functionally diverse molecules in biology. They perform many important functions through their unique three-dimensional structures, which are determined by their sequences of amino acids. Proteins fold into complex shapes through interactions between amino acid side chains within their primary, secondary, tertiary, and sometimes quaternary structures. Changes in a protein's amino acid sequence or structure can significantly impact its function in the cell.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    42 views25 pages

    6 Proteins - Intro

    Uploaded by

    emanuel coates
    Proteins are the most structurally and functionally diverse molecules in biology. They perform many important functions through their unique three-dimensional structures, which are determined by their sequences of amino acids. Proteins fold into complex shapes through interactions between amino acid side chains within their primary, secondary, tertiary, and sometimes quaternary structures. Changes in a protein's amino acid sequence or structure can significantly impact its function in the cell.

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    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    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
     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)
    AP Biology
    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

    Rubisco growth
    AP Biology
    hormones
    Amino acids
     Structure H O
    H | ||
     central carbon
     amino group
    —N—
    —C— C—OH
     carboxyl group (acid) H |
     R group (side chain)
    R
     variable group Oh, I get it!
     different for each amino acid amino = NH2
    acid = COOH
     confers unique chemical
    properties to each amino acid
     like 20 different letters of an
    alphabet
    AP Biology  can make many words (proteins)
    Effect of different R groups:
    Nonpolar amino acids
     nonpolar & hydrophobic

    Why are these nonpolar & hydrophobic?


    AP Biology
    Effect of different R groups:
    Polar amino acids
     polar or charged & hydrophilic

    AP Biology
    Why are these polar & hydrophillic?
    Ionizing in cellular waters H+ donors

    AP Biology
    H+ acceptors
    Ionizing in cellular waters

    AP Biology
    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
     C–N bond

    H2O
    dehydration synthesis

    peptide
    AP Biology 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 protein’s


    structure & its function
     even just one amino acid change
    can make all the difference!

    lysozyme: enzyme in
    tears & mucus that
    AP Biology kills bacteria
    Just 1
    Sickle cell anemia out of 146
    amino acids!

    I’m But I’m


    hydrophilic! hydrophobic!
    AP Biology
    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
    sulfurs in sulfhydryls (S–H)
    AP Biology  anchors 3-D shape
    Quaternary (4°) structure
     More than one polypeptide chain bonded
    together
     only then does polypeptide become
    functional protein
     hydrophobic interactions

    collagen
    AP Biology = skin & tendons hemoglobin
    Protein structure (review)

    R groups
    hydrophobic interactions
    disulfide bridges
    (H & ionic bonds)
    3°
    multiple
    polypeptides
    1° hydrophobic
    amino acid interactions
    sequence 4°
    peptide bonds

    determined 2°
    by DNA R groups
    AP Biology
    H bonds
    In Biology,
    Protein denaturation size doesn’t matter,
    SHAPE matters!
     Unfolding a protein
     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
    X some
    Let’s build

    Proteins!

    AP Biology 2008-2009
    Ghosts of Lectures Past
    (storage)

    AP Biology 2007-2008
    Chaperonin proteins
     Guide protein folding
     provide shelter for folding polypeptides
     keep the new protein segregated from
    cytoplasmic influences

    AP Biology
    Protein models
     Protein structure visualized by
     X-ray crystallography
     extrapolating from amino acid sequence

     computer modelling

    lysozyme
    AP Biology

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