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      Biomolecules (Chemistry)

    Classification of Carbohydrates & Glucose - Preparation and Structure

    • Carbohydrates are called saccharides.

    • Classification

    Classification of Monosaccharides

    • Monosaccharides are classified based on the number of carbon atoms and the functional group present in them.

    • Different types of monosaccharides arelisted in the given table.

    Carbon atoms General term Aldehyde Ketone

    3 Triose Aldotriose etotriose

    ! Tetrose Aldotetrose etotetrose

    " #entose Aldopentose etopentose

    $ %e&ose Aldohe&ose etohe&ose

    ' %eptose Aldoheptose etoheptose

    Glucose

    • Preparation of glucose

    • By boiling sucrose ith dilute %Cl or %*+! in alcoholic solution

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    • By boiling starch ith dilute %*+!, at 3-3 , under pressure

    • Structure

    • lucose has been assigned the above structure based on the folloing evidences.

    (i) Molecular formula / C$%0+$

    (ii) *uggestion of straight chain

    (iii) Confirmation of carbonyl (1 C 2 +) group

    (iv) Confirmation of the presence of carbonyl group as aldehydic group

    (v) Confirmation of the presence of five /+% groups

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    (vi) ndication of the presence of a primary alcohol

    • The correct configuration of glucose is given by

    • lucose is correctly named as D (4) / lucose

    Cyclic Structure of Glucose

    • The folloing reactions of glucose cannot be e&plained by its open5chain structure.

    • Aldehydes give , !5D6# test, *chiff7s test, and react ith 6a%*+ ! to form the hydrogen sulphite addition product. %oever, glucose does not

    undergo these reactions.

    • The penta5acetate of glucose does not react ith hydro&ylamine. This indicates that a free /C%+ group is absent from glucose.

    • lucose e&ists in to crystalline forms, α and  β .

    The α5form (m.p 2 !0- ) crystallises from a concentrated solution of glucose at 383 and the  β 5form (m.p 2 !3 ) crystallises from a hot and saturated

    a9ueous solution at 3'0 . This behaviour cannot be e&plained by the open5chain structure of glucose.

    • lucose e&ists in to cyclic forms, hich e&ist in e9uilibrium ith the open5 chain structure.

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    • :epresentation of the cyclic structure of glucose by %aorth structure;

     Structure of Fructose, Disaccharides & Polysaccharides

    Structure of Fructose

    • +pen5chain structure;

    • Cyclic structure;

    • :epresentation of the structure of fructose by %aorth structures

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    Disaccharides

    lycosidic lin

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    • Lactose

    • Commonly consists of to components / amylase and amylopectin

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    • Cellulose

    • #redominant constituent of the cell all of plant cells.

    • *traight5chain polysaccharide, composed of only  β 5D5lucose

    • Glycogen

    • *torage5polysaccharide in animal body

    • Also

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    • *ome amino acids ith their symbols are listed in the given table.

    Name Side chain ! "hree#letter symbol $ne#letter code

    0. lycine % ly

    . Alanine / C%3 Ala A

    3. ?aline (%3C)C%/ ?al ?

    !. =eucine (%3C)C%/ C%/ =eu =

    ". solecucine le

    $. =ysine % 6/ (C%)! / =ys  

    '. lutamic acid %++C / C%/ C%/ lu @

    . Aspartic acid %++C / C%/ Asp D

    -. Cysteine %* / C% / Cys C

    08. Methionine %3C/ C% / C%/ Met M

    00. #henylalanine C$%"/C% / #he

    0. Tryptophan Trp

    Classification of Amino Acids

    • Based on the relative number of amino and carbo&yl groups, they are classified as acidic, basic and neutral.

    •  6on5essential amino acids;

    • Amino acids that can be synthesised in the body

    • @&ample / lycine, alanine, glutamic acid

    • @ssential amino acids;

    • Amino acids that cannot be synthesised in the body, and must be obtained through diet

    • @&ample / ?aline, leucine, isolecuine

    Properties of Amino Acids

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    • Colourless and crystalline solids

    • @&ist as dipolar ions,

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    • F5heli& structure of protein is as follos;

    o G5pleated sheet structure of proteins is as follos;

    •Tertiary structure of proteins; +verall folding of the polypeptide chains> results in fibrous and globular proteins> secondary and tertiary structuresof proteins are stabilised by hydrogen bonds, disulphide lin

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    Denaturation of Proteins

    • =oss of biological activity of proteins due to the unfolding of globules and uncoiling of heli&.

    • @&ample / Coagulation of egg hite on boiling, curdling of mil

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    Name of (itamins Sources Deficiency diseases

    ?itamin A ish liver oil, car rots,

     butter and mil

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    • Bases in D6A; Adenine (A), guanine (), cytosine (C) and thymine (T)

    • Bases in :6A; Adenine (A), guanine (), cytosine (C) and uracil (L)

    • Structure of nucleic acids

    o *tructure of a nucleoside;

    • *tructure of a nucleotide;

    • ormation of a di5nucleotide;

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    o n secondary structure, the helices of D6A are double5stranded hile those of :6A are single5stranded.

    • The to strands of D6A are complementary to each other.

    :eason; %5bonds are formed beteen specific pairs of bases.

    • Double5strand heli& structure of D6A;

    • Types of :6A;

    • Messenger :6A (m5:6A)

    • :ibosomal :6A (r5:6A)

    • Transfer :6A (t5:6A)

    • unctional differences beteen :6A and D6A;

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    5 !NA DNA

    0. D6A is not responsible for heredity. D6A is the chemical basis of heredity.

    .#roteins are synthesised by :6A molecules in

    the cells.

    D6A molecules do not synthesise proteins, but transfer coded messages for the synthesis

    of proteins in the cells.