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प्रश्न
Discuss the optical activity of lactic acid.
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उत्तर
(1) Lactic acid contains one asymmetric carbon atom which is attached to four different groups, COOH, CH3, OH and H.
(2) Two different arrangements of these groups around the carbon atom are possible as shown in the figure. Hence, it exist as a pair of enantiomers. The two enantiomers are mirror images of each other and are non-superimposable.
(3) Hence, lactic acid can exist in two different forms, d-Form and l-form, which are non-superimposable mirror images of each other. d-form rotates the plane of plane-polarized light to the right, while l-form rotates the same to the left.
(4) A mixture containing equimolar amounts of the d- and l-forms is a racemic mixture which is optically inactive (dl - form). This inactivity arises due to external compensation.
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संबंधित प्रश्न
Define the following as related to proteins:
Peptide linkage
What type of bonding helps in stabilising the α-helix structure of proteins?
Differentiate between the following:
Fibrous proteins and Globular proteins
Differentiate between the following :
Peptide linkage and Glycosidic linkage
Which of the following biomolecules is insoluble in water?
The protein responsible for blood clotting is ____________.
The helical structure of protein is stabilized by:
Proteins are found to have two different types of secondary structures viz. α-helix and β-pleated sheet structure. α-helix structure of protein is stabilised by:
Dinucleotide is obtained by joining two nucleotides together by phosphodiester linkage. Between which carbon atoms of pentose sugars of nucleotides are these linkages present?
Optical rotations of some compounds along with their structures are given below which of them have D configuration.
| (I) |  |
| (II) |  |
| (III) |  |
Proteins can be classified into two types on the basis of their molecular shape i.e., fibrous proteins and globular proteins. Examples of globular proteins are:
(i) Insulin
(ii) Keratin
(iii) Albumin
(iv) Myosin
In fibrous proteins, polypeptide chains are held together by:
(i) van der Waals forces
(ii) disulphide linkage
(iii) electrostatic forces of attraction
(iv) hydrogen bonds
α-Helix is a secondary structure of proteins formed by twisting of polypeptide chain into right-handed screw like structures. Which type of interactions are responsible for making the α-helix structure stable?
Protein found in a biological system with a unique three-dimensional structure and biological activity is called a native protein. When a protein in its native form, is subjected to a physical change like change in temperature or a chemical change like, change in pH, denaturation of protein takes place. Explain the cause.
Which moieties of nucleosides are involved in the formation of phosphodiester linkages present in dinucleotides? What does the word diester in the name of linkage indicate? Which acid is involved in the formation of this linkage?
Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?
The main structural feature of proteins is
Each polypeptide in a protein has amino acids linked with each other in a specific sequence. This sequence of amino acids is said to be ______.
Presence of disulphide link gives rise to which structure of protein?
Out of the following, which type of interaction is responsible for the stabilisation of the α-helix structure of proteins?
The correct structure of Ruhemann's Purple, the compound formed in the reaction of ninhydrin with proteins is:
An α-helix is a structural feature of ______.
What is the effect of denaturation on the structure of proteins?
Write a classification of proteins with an example.
Match List I with List II:
| List I | List II |
| A. GLUT-4 | I. Hormone |
| B. Insulin | II. Enzyme |
| C. Trypsin | III. Intercellular ground substance |
| D. Collagen | IV. Enables glucose transport into cells |
Choose the correct answer from the options given below:
