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A tetrapeptide has -COOH group on alanin...

A tetrapeptide has `-COOH` group on alanine. This produces glycine (Gly), valine (Val), phenyl alanine (Phe) and alanine (Ala), on complete hydrolyses. For this tetrapeptide, the number of possible sequences (primary structures) with `-NH_(2)` group attached to a chiral centre is

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Tetrapeptide is made of naturally occuring alanine , serine, glycine and valine . If the C-terminal amino acid is alanine and the N-terminal amino acid is chiral , the number of possible sequences of the tetrapeptide is

Monosaccharides are polyhydric aldehydes and ketones which cannot be hydrolysed into simpler carbohydrates. The monosaccharides containing -CHO group are called aldoses while those containing C=O group are called ketoses. The aldehyde group is always present at C_(1) while keto group is generally present at C_(2) . All monosaccharides are oxidised by Tollen's reagent and Fehling solution and are called reducing sugars. The monosaccharide molecules may be assigned D and L-configurations depending upon whether the configuration of the molecule is related to D- or L-glyceraldehyde. If the -OH group is attached to the carbon adjacent to the -CH_(2)OH group (last chiral carbon) is on the right hand side, it is assigned D-configuration. The molecule is assigned L-configuration if the -OH group attached to the carbon adjacent to the -CH_(2)OH group is on the left. The monosaccharides contain one or more chiral carbon atoms. Pentoses and hexoses have cyclic structures furanose (five membered) and pyranose (six membered). During cyclization, C_(1) in aldohexoses and C_(2) in fructose become chiral and the newly formed -OH group may be either on the left or on the right in Fischer projection formulae. These monosaccharides, therefore, exist in two stereoisomeric forms called alpha -anomer and beta -anomer while C_(1) and C_(2) are called glycosidic or anomeric carbon. The bonds joining glycosidic carbon are called glycosidic linkages. D(+) glucose exists in two stereoisomeric forms, alpha -D- glucose and beta -D-glucose. When either of these two forms of glucose i.e., alpha-D- glucose are dissolved in water and allowed to stand, these get slowly converted into other form and an equilibrium mixture of both is formed. This process is called mutarotation. The maximum number of optical isomers of glucose expected are

A hexapeptide has the composition Ala,Gly,Phe,Val. Both the N- terminal and C- teminal units are Val. Cleavage of the hexapeptide by chymotypsin gives two different tripeptides, both having Val as the N-terminal group. Among the products of random hydrolysis is a Ala-Val dipeptide fragment . What is the primary structure of the hexapeptide?

Proteins are high molecular mass complex biomolecules of amino acids. The important proteins required for our body are enzymes, hormones, antibodies, transport proteins, structural proteins, contractile proteins etc. Except for glycine, all alpha -amino acids have chiral carbon atom and have L-configuration. The amino acids exists as dipolar ion called zwitter ion, in which a proton goes from the carboxyl group to the amino group. A large number of alpha -amino acids are joined by peptide bonds forming polypeptides. The peptides having very large molecular mass (more than 10,000) are called proteins. The structure of proteins is described as primary structure giving sequence of linking of amino acids, secondary structure giving manner in which polypeptide chains are arranged and folded, tertiary structure giving folding, coiling or bonding polypeptide chains producing three dimensional structures and quaternary structure giving arrangement of sub-units in an aggregate protein meolecule. Which of the following alpha -amino acid does not form optical isomers?

Proteins are high molecular mass complex biomolecules of amino acids. The important proteins required for our body are enzymes, hormones, antibodies, transport proteins, structural proteins, contractile proteins etc. Except for glycine, all alpha -amino acids have chiral carbon atom and have L-configuration. The amino acids exists as dipolar ion called zwitter ion, in which a proton goes from the carboxyl group to the amino group. A large number of alpha -amino acids are joined by peptide bonds forming polypeptides. The peptides having very large molecular mass (more than 10,000) are called proteins. The structure of proteins is described as primary structure giving sequence of linking of amino acids, secondary structure giving manner in which polypeptide chains are arranged and folded, tertiary structure giving folding, coiling or bonding polypeptide chains producing three dimensional structures and quaternary structure giving arrangement of sub-units in an aggregate protein meolecule. Which of the following statements is not correct?

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