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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 structu - Chemistry

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प्रश्न

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?

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उत्तर

In α-helix structure of protein, a polypeptide chain is stabilize by the formation of intramolecular H – bonding between – NH – group of amino acids in one turn with the >C = O groups of amino acids belonging to adjacent turn.

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अध्याय 14: Biomolecules - Multiple Choice Questions (Type - I) [पृष्ठ २१०]

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एनसीईआरटी एक्झांप्लर Chemistry [English] Class 12
अध्याय 14 Biomolecules
Multiple Choice Questions (Type - I) | Q 39 | पृष्ठ २१०

संबंधित प्रश्न

How are proteins classified on the basis of molecular shapes?


Differentiate between the following :

Peptide linkage and Glycosidic linkage 


Which of the following biomolecules is insoluble in water?


The correct statement for protein haemoglobin.


Which functional group participates in disulphide bond formation in proteins?


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:


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


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?


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 total number of negative charge in the tetrapeptide, Gly-Glu-Asp-Tyr at pH 12.5 will be ______. (Integer answers)


An α-helix is a structural feature of ______.


Assertion (A): Proteins are polymers of α-amino acids connected by a peptide bond.

Reason (R): A tetrapeptide contains 4 amino acids linked by 4 peptide bonds.


β-pleated sheet structure in proteins refers to ______.


What is the effect of denaturation on the structure of proteins?


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