Secondary Structure of Proteins
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- Lysine, Arginine
- Alanine, Glutamic acid
- Proline, Valine
- Alanine, Cysteine
- Lysine
- Proline
- Alanine
- Aspartic acid
All Amino acids exist as Zwitter ions.
Reason
Amino acids have both- NH2 and - COOH group.
- Both Assertion and Reason are correct and Reason is the correct explanation for Assertion
- Both Assertion and Reason are correct but Reason is not the correct explanation for Assertion
- Assertion is correct but Reason is incorrect
- Both Assertion aand Reason are incorrect
The α - amino acids, usually exist in the form of zwitter ions. It means they have:
No acidic or basic group
Basic group - COO- and acidic group NH4+
Basic group -COO- and acidic group - NH3+
Basic group - COO- and acidic group - COO2-
QUESTION 14.14
What type fo bonding helps in stabilising the α - helix structure fo proteins?
α− helix is a secondary structure of proteins formed by twisting of polypeptide chain into right handed screw like structure. Which type of interactions are responsible for making the α− helix structure stable?
Globular proteins are highly branched proteins usually soluble in water.
Reason
Insulin and Albumin are the common fibrous proteins.
- Both Assertion and Reason are correct and Reason is the correct explanation for Assertion
- Both Assertion aand Reason are correct but Reason is not the correct explanation for Assertion
- Assertion is correct but Reason is incorrect
- Both Assertion and Reason are incorrect
α - helix structure of protein is stabilized by
Peptide bond
Vander Waals forces
Hydrogen bond
Dipole - dipole interactions
QUESTION 14.13
What are the common types of secondary structure fo proteins?
- α-helix
- β-pleated sheet
- tertiary structure
- None of the above
- H-bond
- Ionic bond
- Covalent bond
- Vander Waals forces
- dipeptide
- tripeptide
- tetrapeptide
- polypeptide
- Proline
- Histidine
- Valine
- Methionine
- If the polypeptide chain is held together by disulphide bridges and combine to form fibre like structure, then it is called fibrous protein.
- Examples for fibrous proteins are keratin, elastin, myosin, etc, .
- Fibrous proteins have a coil like structure.
- Fibrous proteins are insoluble in water.
- Non-essential amino acids are synthesized in the body
- Most naturally occuring amino acids have D-configuration
- Glycine is the only optically inactive among naturally occuring α amino acids
- Amino acids show amphoteric behaviour in zwitter ionic form
- α− helix and β− helix structures
- α− helix and β− pleated structures
- right and left hand twisted structures
- globular and fibrous structures
α - helix structure of protein is stabilized by
Peptide bond
Vander Waals forces
Hydrogen bond
Dipole - dipole interactions
- Sequence of α-amino acids
- α-helical backbone
- Hydrophobic interactions
- Fixed configuration of the polypeptide backbone
- Serine
- Lysine
- Alanine
- Tyrosine
(JEE MAIN 2021)
- Covalent bonding
- vander Waals forces
- Hydrogen bonding
- Ionic bonding
Describe the secondary structure of proteins.
α - helix structure of protein is stabilized by
Peptide bond
Vander Waals forces
Hydrogen bond
Dipole - dipole interactions
- peptide bonds
- van der Waals forces
- hydrogen bonds
- none of these
- Myosin
- Collagen
- Keratin
- All of these
- If the polypeptide chain is held together by disulphide bridges and combine to form fibre like structure, then it is called fibrous protein.
- Examples for fibrous proteins are keratin, elastin, myosin, etc, .
- Fibrous proteins have a coil like structure.
- Fibrous proteins are insoluble in water.
- Myosin
- Collagen
- Keratin
- All of these