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    Amino Acid

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    Shankar Shahi
    This document discusses amino acids, peptides, and proteins. It begins by describing the basic structure of amino acids, including that they contain an amine group, carboxyl group, and R group side chain. It then lists the 20 common amino acids found in proteins and provides their structures. The document discusses how amino acids join together via peptide bonds to form peptides and proteins. It covers the four levels of protein structure - primary, secondary, tertiary, and quaternary. Finally, it classifies proteins into simple proteins and conjugated proteins and provides examples.

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    © All Rights Reserved
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    Amino Acid

    Uploaded by

    Shankar Shahi
    176 views33 pages
    This document discusses amino acids, peptides, and proteins. It begins by describing the basic structure of amino acids, including that they contain an amine group, carboxyl group, and R group side chain. It then lists the 20 common amino acids found in proteins and provides their structures. The document discusses how amino acids join together via peptide bonds to form peptides and proteins. It covers the four levels of protein structure - primary, secondary, tertiary, and quaternary. Finally, it classifies proteins into simple proteins and conjugated proteins and provides examples.

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    This document discusses amino acids, peptides, and proteins. It begins by describing the basic structure of amino acids, including that they contain an amine group, carboxyl group, and R group side chain. It then lists the 20 common amino acids found in proteins and provides their structures. The document discusses how amino acids join together via peptide bonds to form peptides and proteins. It covers the four levels of protein structure - primary, secondary, tertiary, and quaternary. Finally, it classifies proteins into simple proteins and conjugated proteins and provides examples.

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    176 views33 pages

    Amino Acid

    Uploaded by

    Shankar Shahi
    This document discusses amino acids, peptides, and proteins. It begins by describing the basic structure of amino acids, including that they contain an amine group, carboxyl group, and R group side chain. It then lists the 20 common amino acids found in proteins and provides their structures. The document discusses how amino acids join together via peptide bonds to form peptides and proteins. It covers the four levels of protein structure - primary, secondary, tertiary, and quaternary. Finally, it classifies proteins into simple proteins and conjugated proteins and provides examples.

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    of 33

    AMINO ACIDS, PEPTIDE &

    PROTEIN
    Amino acids are building units of proteins.
    Amino acids are organic compounds having an
    amine group(NH2) and carboxylic group (COOH)
    attached to the alpha carbon molecules with
    side chain R-group and hidrogen molecule.
    Amino acid consist of:
    A) hydrogen atom
    B)Carboxylic group
    C)Amino group NH2
    D)Side chain R group

    20 alpha amino acids


    Name
    Alanine

    Abbreviation/Alp Linear Structure


    habetic code
    Ala, A
    CH3-CH(NH2)-COOH

    Arginine

    Arg,R

    Asparagine Asn,N

    HN=C(NH2)-NH-(CH2)3CH(NH2)-COOH
    H2N-CO-CH2-CH(NH2)-COOH

    Aspartic Aci Asp,D


    d
    Cysteine
    Cys,C

    HOOC-CH2-CH(NH2)-COOH

    Glutamic Ac Glu,E
    id
    Glutamine Gln,Q

    HOOC-(CH2)2-CH(NH2)-COOH

    Glycine

    Gly,G

    NH2-CH2-COOH

    Histidine

    His,H

    NH-CH=N-CH=C-CH2-CH(NH2)COOH

    HS-CH2-CH(NH2)-COOH
    H2N-CO-(CH2)2-CH(NH2)-COOH

    Cont.
    Name
    Isoleucine

    Abbreviation Linear Structure


    Ile,I
    CH3-CH2-CH(CH3)CH(NH2)-COOH
    Leucine
    Leu,L
    (CH3)2-CH-CH2-CH(NH2)COOH
    Lysine
    Lys,K
    H2N-(CH2)4-CH(NH2)COOH
    Methionine Met,M
    CH3-S-(CH2)2-CH(NH2)COOH
    Phenylalani Phe,F
    Ph-CH2-CH(NH2)-COOH
    ne
    Proline
    Pro,P
    NH-(CH2)3-CH-COOH
    Serine
    Ser,S
    HO-CH2-CH(NH2)-COOH
    Threonine
    Thr,T
    CH3-CH(OH)-CH(NH2)COOH
    Tryptophan Trp,W
    Ph-NH-CH=C-CH2CH(NH2)-COOH

    Biomedical important of amino


    acids
    Amino acids serve as a building blocks of proteins.
    Some amino acids are found in free form in human
    blood.
    They also serve as precursors of hormones, purines,
    pyrimidines, prophyrins, vitamins.
    Peptides have many important biological functions
    some of them are hormones they are used as
    antibiotics and antitumor agents.
    Some peptides are required for detoxification
    reactions. Some peptides serve as neurotransmitters.
    Some synthetic peptides are used as enzyme
    substrates.

    Classification of amino acids:


    Based on the chemical structure:
    Based on the Nature of the Rgroup( polarity)
    Based on the Nutritional Requirement
    Based on the Metabolic Fate.

    Based on the chemical structure:


    A) Aliphatic amino acids e.g. Glycin.
    Alanine
    B) Hydroxy amino acids: amino acids that
    contain OH group in R-side chain.
    e.g. Serine, Threonine
    C) Sulphur containing amino acids: amino
    acids that contain SH group in R-side chain.
    e.g. Cysteine, Metheonine

    D ) Amide group containing amino acids:


    amino acids that contain NH2 group in Rside chain. e.g. Glutamine, Asparagine
    E) Acidic amino acids:
    monoamino,dicarboxylic amino acids. E.g.
    Glutamic acid, Aspartic acid
    F) Basic amino acids: Diaaminno
    monocarboxylic aminno acids. E.g. Lysine,
    arginine

    G) Aromatic amino acids: amino acids


    containing aromatic ring e.g.
    Phenylalanine, Tyrosine,Tryptophan

    Classification on the basis of polarity


    1) Non polar amino acids Risalkylhydrophobicgroupwhichcantenterin
    hydrogenbondformation.9aminoacidsarenonpolar(glycine,alanine,valine,leucine,
    isoleucine,phenylalanine,tryptophan,prolineandmethionine)
    Glycine
    (Gly)
    Alanine
    (Ala)

    Methionine (Met)

    Phenylalanine (Phe)

    Valine (Val)
    Tryptophan (Trp)
    Leucine
    (leu)

    2) Polar amino acids with no charge on r group: InwhichR


    containspolarhydrophilicgroupsocanformshydrogenbondwithH 2O.Inthoseaminoacids,R
    maycontain:

    1OH group :asinserine,threonineandtyrosine


    2- SH group :asincysteine
    3- amide group: asinglutamineandaspargine
    4- NH2 group or nitrogen act as a base (basic amino acids ): aslysine,arginineandhistidine
    5- COOH group ( acidic amino acids): asasparticandglutamic.

    Serine (Ser)

    Cysteine
    (cys)

    Threonine (Thr)

    Asparagine (Asn)

    Tyrosine (Tyr)

    Glutamine (Gln)

    3) Polar amino acid with positive r group

    Lysine (Lys)

    Arginine (Arg)

    Histidine (His)

    4) Polar amino acid with negative R


    group
    Aspartic acid (Asp)

    Glutamic acid (Glu)

    Classification on the basis of Nutritional


    Requirements

    Eesential amino acids These cannot


    be synthesized in the body. Therefore
    they must be supplied through the diet.
    Arginine*
    Histidine*
    Isoleucine
    Leucine
    Valine

    Lysine
    Methionine
    Threonine
    Phenylalanin
    e
    Tryptophan
    (TAMP
    HILL TV)

    * Can be synthesized by adults but not by


    growing
    children. They are also called as
    semi essential amino acids.

    Non essential amino acids


    They are synthesized in our body.
    Hence they need not to be
    consumed in the diet.
    Alanine
    Asparagine
    Aspartate
    Glutamate
    Glutamine

    Glycine
    Proline
    Serine
    Cysteine
    Tyrosine

    (3GPATACAS)

    Classification on the basis of metabolic


    fate:
    1) Glycogenic amino acid
    these amino acids serve as a
    precursor for the formation of
    glucose or glycogen.
    eg. alanine, aspartate, glycine,
    methionine etc.
    2) Ketogenic amino acid fat
    can be synthesized from these
    amino acids.
    eg. Lucine and lysine

    Properties of amino acids

    Solubility: most of the amino acids are soluble in water and


    insoluble in organic solvents.

    Melting point: melt at higher temperature


    (above 200 c)

    Taste: sweet - glycine, alanine, valine


    tasteless leucine
    bitter arginine, isoleucine
    Optical activity: all the amino acids except glycine possess

    optical isomers due to presence of asymmetric carbon atom.

    glycine

    Peptides and Proteins


    20 amino acids are commonly found in
    protein. These 20 amino acids are linked
    together through peptide bond forming
    peptides and proteins .
    - The chains containing less than 50 amino
    acids are called peptides, while those
    containing greater than 50 amino acids are
    called proteins.

    Formation of peptide bond:


    -carboxyl group of one amino acid (with side chain R1) forms a
    covalent peptide bond with -amino group of another amino acid
    ( with the side chain R2) by removal of a molecule of water. The
    result is Dipeptide ( i.e. Two amino acids linked by one peptide
    bond). By the same way, the dipeptide can then forms a second
    peptide bond with a third amino acid (with side chain R3) to give
    Tripeptide. Repetition of this process generates a polypeptide or
    protein of specific amino acid sequence.

    Each polypeptide chain starts on the left side by free amino group of the
    first amino acid enter in chain formation . It is termed (N- terminus).
    - Each polypeptide chain ends on the right side by free COOH group of
    the last amino acid and termed (C-terminus).

    Examples on Peptides:
    1- Dipeptide ( tow amino acids joined by one peptide
    bond): Example: Aspartame which acts as sweetening
    agent being used in replacement of cane sugar. It is
    composed of aspartic acid and phenyl alanine.
    2- Tripeptides ( 3 amino acids linked by two peptide
    bonds). Example: GSH which is formed from 3 amino acids:
    glutamic acid, cysteine and glycine. It helps in absorption of
    amino acids, protects against hemolysis of RBC by breaking
    H2O2 which causes cell damage.
    3- Octapeptides: (8 amino acids)
    Examples: Two hormones; oxytocine and vasopressin (ADH).
    4- polypeptides: 10- 50 amino acids: e.g. Insulin hormone

    Protein Structure:
    There are four levels of protein
    structure (primary, secondary, tertiary
    and quaternary)
    Primary structure:
    The primary structure of a protein is
    its unique sequence of amino acids..
    The precise primary structure of a
    protein is determined by inherited
    genetic information.
    At one end is an amino acid with a
    free amino group the (the N-terminus)
    and at the other is an amino acid with
    a free carboxyl group the (the Cterminus).

    2- Secondary structure: Results


    from hydrogen bond formation
    between hydrogen of NH group of
    peptide bond and the carbonyl
    oxygen of another peptide bond.
    According to H-bonding there are
    two main forms of secondary
    structure:
    -helix: It is a spiral structure
    resulting from hydrogen bonding
    between one peptide bond and the
    fourth one
    -sheets: is another form of
    secondary structure in which two or
    more polypeptides linked together
    by hydrogen bond.

    Tertiary structure is determined by a


    variety of interactions (bond formation)
    between R groups and the polypeptide
    backbone. The 3-dimensional structure of
    a protein's polypeptide chain may be
    locked in place by other stronger bonds.
    a. The weak interactionsinclude:
    Hydrogen bonds
    Ionic bonds
    Hydrophobic interactions
    b. Strong covalent bonds include
    disulfide bridges, that form between
    the sulfhydryl groups (SH) of cysteine
    monomers, stabilize the structure.

    Quaternary structure: results from the


    combination of two or more polypeptide subunits
    held together by non-covalent interaction like Hbonds, ionic or hydrophobic interactions.
    Examples on protein having quaternary structure:
    Collagen is a fibrous protein of three
    polypeptides (trimeric).
    Hemoglobin is a globular protein with four
    polypeptide chains(tetrameric)
    Insulin : two polypeptide chains (dimeric)

    Classification of proteins
    I- Simple proteins:
    i.e. on hydrolysis gives only amino acids
    Examples:
    1- Albumin and globulins: present in egg, milk and blood They are
    proteins of high biological value i.e. contain all essential amino acids
    and easily digested.
    Types of globulins:
    1 globulin: e.g. antitrypsin
    2 globulin: e.g. hepatoglobin: protein that binds hemoglobin to
    prevent its excretion by the kidney
    -globulin: e.g. transferrin: protein that transport iron
    -globulins = Immunoglobulins (antibodies) : responsible for immunity.

    - Globins (Histones): They are basic proteins rich in histidine amino


    acid.
    They are present in :
    a - combined with DNA
    b - combined with heme to form hemoglobin of
    RBCs.
    - Scleroproteins: They are structural proteins, not digested. include:
    keratin, collagen and elastin.
    a- -keratin: protein found in hair, nails, enamel of teeth and outer layer
    of skin.
    It is rich in cysteine and hydrophobic (non polar) amino acids so it is
    water insoluble.
    b- collagens: protein of connective tissues found in bone, teeth,
    cartilage, tendons, skin and blood vessels.

    Conjugated proteins
    1- Lipoproteins:
    These are proteins conjugated with lipids. E.g. HDL,LDL, VLDL
    2- Phosphoproteins: protein+ phosphate
    3- Glycoproteins:
    proteins conjugated with sugar (carbohydrate)
    e.g. Mucin
    - Some hormones such as erythropoeitin
    - present in cell membrane structure
    - blood groups antigens
    4- Nucleoproteins: These are basic proteins ( e.g. histones)
    conjugated with nucleic acid (DNA or RNA).
    e.g. a- chromosomes: are proteins conjugated with DNA
    b- Ribosomes: are proteins conjugated with RNA

    5- Metalloproteins: These are proteins conjugated with


    metal like iron, copper, zinc,
    a- Iron-containing proteins: Iron may present in heme
    such as in
    - hemoglobin (Hb)
    - myoglobin ( protein of skeletal muscles and
    cardiacmuscle),
    - cytochromes,
    - catalase, peroxidases (destroy H2O2)

    b- Copper containing proteins:


    e.g. - Ceruloplasmin which oxidizes ferrous ions into ferric ions.
    - Oxidase enzymes such as cytochrome oxidase.

    -Chromoproteins: These are proteins conjugated


    with pigment. e.g.
    - All proteins containing heme (Hb, myoglobin, ..)
    - Melanoprotein:e.g proteins of hair or iris
    which contain melanin.

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