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कर्नाटक बोर्ड पी.यू.सी.पीयूसी विज्ञान 2nd PUC Class 12

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

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प्रश्न

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

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उत्तर

(i) Insulin

(iii) Albumin

Explanation:

This structure results when the chain of polypeptides coil around to give a spherical shape. These are usually soluble in water. Insulin and albumin are the common examples of globular proteins.

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अध्याय 14: Biomolecules - Multiple Choice Questions (Type - I) [पृष्ठ २०७]

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एनसीईआरटी एक्झांप्लर Chemistry Exemplar [English] Class 12
अध्याय 14 Biomolecules
Multiple Choice Questions (Type - I) | Q 21 | पृष्ठ २०७

संबंधित प्रश्न

What are the common types of secondary structure of proteins?


Write one difference between α-helix and β-pleated structures of proteins.


Differentiate between the following :

Peptide linkage and Glycosidic linkage 


The correct statement for protein haemoglobin.


Which functional group participates in disulphide bond formation in proteins?


Which of the following statement is correct:


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)

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.


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 ______.


Explain formation of peptide linkage in protein with an example.


The correct structure of Ruhemann's Purple, the compound formed in the reaction of ninhydrin with proteins is:


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 ______.


Proteins are polymers of ______.


Statement I: A protein is imagined as a line, the left end represented by first amino acid (C-terminal) and the right end represented by last amino acid (Nterminal).

Statement II: Adult human haemoglobin, consists of 4 subunits (two subunits of a type and two subunits β type.)

In the light of the above statements, choose the correct answer from the options given below:


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