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    Protein Notes PDF

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    LUi Anne Mateo Latog
    Proteins are polymers made of amino acid monomers linked by peptide bonds. The 20 standard amino acids are the building blocks of proteins and contain an amino group, a carboxyl group, and a variable R group. Proteins serve many important functions in the body as enzymes, structural components, transport and messenger molecules. They form complex structures like alpha helices and beta sheets through interactions between R groups. Proteins can be classified based on size, shape, number of polypeptide chains, and presence of non-amino acid components. Denaturation involves disruption of the secondary, tertiary and quaternary structure through heat, pH, chemicals or agitation.

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    Protein Notes PDF

    Uploaded by

    LUi Anne Mateo Latog
    384 views38 pages
    Proteins are polymers made of amino acid monomers linked by peptide bonds. The 20 standard amino acids are the building blocks of proteins and contain an amino group, a carboxyl group, and a variable R group. Proteins serve many important functions in the body as enzymes, structural components, transport and messenger molecules. They form complex structures like alpha helices and beta sheets through interactions between R groups. Proteins can be classified based on size, shape, number of polypeptide chains, and presence of non-amino acid components. Denaturation involves disruption of the secondary, tertiary and quaternary structure through heat, pH, chemicals or agitation.

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    Proteins are polymers made of amino acid monomers linked by peptide bonds. The 20 standard amino acids are the building blocks of proteins and contain an amino group, a carboxyl group, and a variable R group. Proteins serve many important functions in the body as enzymes, structural components, transport and messenger molecules. They form complex structures like alpha helices and beta sheets through interactions between R groups. Proteins can be classified based on size, shape, number of polypeptide chains, and presence of non-amino acid components. Denaturation involves disruption of the secondary, tertiary and quaternary structure through heat, pH, chemicals or agitation.

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    © All Rights Reserved
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    384 views38 pages

    Protein Notes PDF

    Uploaded by

    LUi Anne Mateo Latog
    Proteins are polymers made of amino acid monomers linked by peptide bonds. The 20 standard amino acids are the building blocks of proteins and contain an amino group, a carboxyl group, and a variable R group. Proteins serve many important functions in the body as enzymes, structural components, transport and messenger molecules. They form complex structures like alpha helices and beta sheets through interactions between R groups. Proteins can be classified based on size, shape, number of polypeptide chains, and presence of non-amino acid components. Denaturation involves disruption of the secondary, tertiary and quaternary structure through heat, pH, chemicals or agitation.

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    PROTEIN

    Mark Raymund G. Nava, RMT, MPA, MSMT


    Assistant Professor
    PROTEIN
    naturally occurring, unbranched polymer
    in which the monomer units are amino
    acids
    peptide in which at least 40 amino acid
    residues are present
    also known as polypeptide
    FUNCTIONS
    contain Carbon, Hydrogen, Oxygen,
    Nitrogen, sometimes Sulfur and
    Phosphorous
    serve as structural components of
    animals
    serve as control molecules (enzymes)
    serve as transport and messenger
    molecules
    AMINO ACIDS
    Building blocks of proteins
    Organic compound that contains both an
    amino group and a carboxyl group
    700 different naturally occurring amino
    acids but only 20 are normally present in
    proteins Standard Amino Acids
    AMINO ACIDS
    AMINO ACIDS
    Amino group acts like a base, tends to be
    positive
    Carboxyl group acts like an acid, tends to
    be negative
    R group is variable, from 1 atom to 20
    two amino acids join together to form a
    dipeptide
    adjacent Carboxyl and Amino groups bond
    together
    SOME AMINO ACIDS
    SOME AMINO ACIDS
    SOME AMINO ACIDS
    CLASSIFICATION
    base on side chain polarity
    Classification Description
    1 amino group
    Non- Polar 1 carboxyl group
    Amino Acids 1 non polar side chain
    1 amino group
    Polar Neutral 1 carboxyl group
    Amino Acids 1 polar neutral side chain
    1 amino group
    Polar Acidic 2 carboxyl group
    Amino Acids (1 is part of side chain)
    2 amino group
    Polar Basic (1 is part of side chain)
    Amino Acids 1 carboxyl group
    CLASSIFICATION
    base on side chain polarity
    NON-POLAR AMINO ACIDS
    POLAR AMINO
    Glycine Gly G
    Alanine Ala A
    ACIDS
    Valine Val V Serine Ser S
    Leucine Leu L Cysteine Cys C
    Isoleucine Ile I Threonine Thr T
    Proline Pro P Asparagine Asn N
    Phenylalanine Phe F
    Glutamine Gln Q
    Methionine Met M
    Tyrosine Tyr Y
    Tryphtopan Trp W
    CLASSIFICATION
    base on side chain polarity
    POLAR ACIDIC AMINO POLAR BASIC AMINO
    ACIDS ACIDS
    Aspartic Histidine His H
    Asp D
    Acid
    Lysine Lys H
    Glutamic
    Glu E Arginine Arg R
    Acid
    ESSENTIAL AMINO ACIDS
    Arginine Methionine
    Histidine Phenylalanine
    Isoleucine Threonine
    Leucine Tryptophan
    Lysine Valine
    CHIRALITY OF AMINO ACIDS
    All 20 standard amino acids have chiral
    centers except GLYCINE
    Hence, amino acids have mirror images:
    Right and Left based on the location of the
    amino group
    Nature favors/prefers the L-isomers of
    amino acids
    CHIRALITY OF AMINO ACIDS

    COOH

    H2N C H

    R
    ACID-BASE PROPERTIES
    OF AMINO ACIDS
    H

    H2N C COOH

    R
    ACID-BASE PROPERTIES
    OF AMINO ACIDS
    Both acidic and basic group are present in
    an -amino acid
    In solution, three different amino acids
    exist: a zwitterion, a negative ion and a
    positive ion
    If in crystal form, not soluble with water
    due to strong intermolecular forces
    ISOELECTRIC POINT
    The pH at which an amino acid has no net
    charge because equal number of positive
    and negative charges are present
    Example:
    alanine - 6.01
    glycine - 5.97
    valine - 5.97
    Formation of a Dipeptide

    Dehydration synthesis
    Amino Acid + Amino Acid Dipeptide

    Amino Acid + Dipeptide Tripeptide


    A.A. + A.A. + ..+ Tripeptide Polypeptide
    Naming Peptides
    IUPAC Rules in naming small peptides

    RULE 1:
    The C-terminal amino acid residue keeps
    its full amino acid name
    Naming Peptides
    IUPAC Rules in naming small peptides
    RULE 2:
    All the other amino acid residue names
    ending in -ine or ic acid will be
    replaced with yl, except:
    Tryphtopan Tryptophyl; Cysteine Cysteinyl;
    Glutamine Glutaminyl; Asparagine - Asparaginyl
    Naming Peptides
    IUPAC Rules in naming small peptides

    RULE 3:
    The amino acid naming sequence begins
    at the N-terminal amino acid residue
    Naming Peptides
    IUPAC Rules in naming small peptides

    EXAMPLE:
    Glu Ser Ala

    glutamyl seryl alanine

    Glutamylserylalanine
    CLASSIFICATION OF PROTEIN
    base on number of peptide chain
    1. MONOMERIC only one peptide chain
    is present

    2. MULTIMERIC more than one peptide


    chain is present
    CLASSIFICATION OF PROTEIN
    base on chemical composition
    1. SIMPLE only amino acid residues are
    present

    2. CONJUGATED one or more non-amino


    acid entities present in its structure in
    addition to one or more peptide chains
    Conjugated Proteins
    Simple Prosthetic Conjugated
    Protein + Group
    = Protein

    Peptide Organic or
    chain Inorganic
    non-amino acid
    component
    Conjugated Proteins
    CLASS PROSTHETIC GROUP EXAMPLE
    Hemoglobin
    Hemoproteins Heme unit Myoglobin
    LDL, HDL, VLDL and
    Lipoproteins Lipids Chylomicrons
    Gamma Globulin
    Glycoproteins Carbohydrate Mucin
    Interferon
    Phosphoproteins Phosphate group Glycogen phosphorylase
    Ribosomes
    Nucleoproteins Nucleic Acids Viruses
    Ferritin
    Metalloproteins Metal Ion Alcohol Dehydrogenase
    STRUCTURE OF PROTEIN
    Alpha Helix
    Beta Pleated Sheets
    CLASSIFICATION OF PROTEIN
    base on shape
    1. FIBROUS have an elongated shape
    with one dimension much longer than
    the others

    2. GLOBULAR have peptide chains folded


    into spherical and globular shapes
    Fibrous Versus Globular Proteins
    FIBROUS GLOBULAR
    Extended protein Compact protein
    structure structure
    Insoluble in water Soluble in water
    Secondary structure is
    Secondary structure is complex mixture of
    simple -helix, -sheet, loop
    structures
    Functions for support
    Functions in all aspects
    and external
    of metabolism
    protection
    Fibrous Versus Globular Proteins
    PROTEIN HYDROLYSIS
    splits peptide bonds to smaller peptides and
    amino acids
    occurs in the digestion of proteins
    occurs in cells when amino acids are needed
    to synthesize new proteins and repair tissues
    In the lab, hydrolysis of a peptide requires acid
    or base, water, and heat
    In the body, enzymes catalyze the hydrolysis of
    proteins
    Hydrolysis of Peptide

    H2O enzymes
    DENATURATION
    involves the disruption of bonds in the
    secondary, tertiary, and quaternary structures
    heat and organic compounds break apart H
    bonds and disrupt hydrophobic interactions
    acids and bases break H bonds between
    polar R groups and disrupt ionic bonds
    heavy metal ions react with SS bonds to
    form solids
    agitation (whipping, shaking) stretches
    peptide chains until bonds break

    37
    Applications of Denaturation
    Cooking eggs
    Wiping of alcohol
    Heat used to cauterize
    blood vessels
    Sterilization of
    instruments in
    autoclave
    Hair perming

    38

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