In proteins the α-helix and β-pleated sheet are examples of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure

In proteins the α-helix and β-pleated sheet are examples of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure
by

1 Answer

Answer :

Answer : B
by
selected

Related questions

Which of the following may characterize the “secondary structure” of proteins? (a) conformation of the protein backbone (b) α-Helix (c) parallel β-pleated sheet (d) all of the above

Description : Which of the following may characterize the “secondary structure” of proteins? (a) conformation of the protein backbone (b) α-Helix (c) parallel β-pleated sheet (d) all of the above

Last Answer : all of the above

In protein structure the α-helix and βpleated sheets are example of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure

Description : In protein structure the α-helix and βpleated sheets are example of (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure

Last Answer : Answer : B

Both α-helix and β-pleated sheet conformation of proteins were proposed by (A) Watson and Crick (B) Pauling and Corey (C) Waugh and King (D) Y.S.Rao

Description : Both α-helix and β-pleated sheet conformation of proteins were proposed by (A) Watson and Crick (B) Pauling and Corey (C) Waugh and King (D) Y.S.Rao

Last Answer : Answer : B

During denaturation of proteins, all of the following are disrupted except (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure

Description : During denaturation of proteins, all of the following are disrupted except (A) Primary structure (B) Secondary structure (C) Tertiary structure (D) Quaternary structure

Last Answer : Answer : B

The linear arrangement of amino acid units in proteins is called : (a) primary structure (b) secondary structure (c) tertiary structure (d) quaternary structure

Description : The linear arrangement of amino acid units in proteins is called : (a) primary structure (b) secondary structure (c) tertiary structure (d) quaternary structure

Last Answer : primary structure

The α-Helix is a common form of (a) Primary structure (b) Tertiary structure (c) Secondary structure (d) None of these

Description : The α-Helix is a common form of (a) Primary structure (b) Tertiary structure (c) Secondary structure (d) None of these

Last Answer : Secondary structure

The a-helix of proteins is (A) A pleated structure (B) Made periodic by disulphide bridges (C) A non-periodic structure (D) Stabilised by hydrogen bonds between NH and CO groups of the main chain

Description : The a-helix of proteins is (A) A pleated structure (B) Made periodic by disulphide bridges (C) A non-periodic structure (D) Stabilised by hydrogen bonds between NH and CO groups of the main chain

Last Answer : Answer : C

The _______ structure of a protein is the sequence of amino acids. a. primary b. secondary c. tertiary d. quaternary

Description : The _______ structure of a protein is the sequence of amino acids. a. primary b. secondary c. tertiary d. quaternary

Last Answer : a. primary

In many proteins the hydrogen bonding produces a regular coiled arrangement which is called as (A) β-Helix (B) α-Helix (C) Both (A) and (B) (D) Spiral

Description : In many proteins the hydrogen bonding produces a regular coiled arrangement which is called as (A) β-Helix (B) α-Helix (C) Both (A) and (B) (D) Spiral

Last Answer : Answer : B

In many proteins the hydrogen bonding produces a regular coiled arrangement called (A) α-helix (B) β-helix (C) Both (A) and (B) (D) None of these

Description : In many proteins the hydrogen bonding produces a regular coiled arrangement called (A) α-helix (B) β-helix (C) Both (A) and (B) (D) None of these

Last Answer : Answer : A

Which one of the following economic sectors is Laxmi related to? (a) Primary (b) Secondary (c) Tertiary (d) Quaternary

Description : Which one of the following economic sectors is Laxmi related to? (a) Primary (b) Secondary (c) Tertiary (d) Quaternary

Last Answer : Take the case of Laxmi with her two-hectare plot of unirrigated land. The government can spend some ... (b) Secondary (c) Tertiary (d) Quaternary

______ form the bulk of microbial products of industrial interest. a. primary metabolites b. secondary metabolites c. tertiary metabolites d. quaternary metabolites

Description : ______ form the bulk of microbial products of industrial interest. a. primary metabolites b. secondary metabolites c. tertiary metabolites d. quaternary metabolites

Last Answer : b. secondary metabolites

Which of the following protein structures does “denaturation” destroy?(a) primary and secondary structures (b) secondary and tertiary structures (c) tertiary and quaternary structures (d) secondary, tertiary, and quaternary structures

Description : Which of the following protein structures does “denaturation” destroy? (a) primary and secondary structures (b) secondary and tertiary structures (c) tertiary and quaternary structures (d) secondary, tertiary, and quaternary structures

Last Answer : secondary, tertiary, and quaternary structures

Which type of amine produces N2 when treated with HONO? (a) Primary (b) Secondary (c) Tertiary (d) Quaternary

Description : Which type of amine produces N2 when treated with HONO? (a) Primary (b) Secondary (c) Tertiary (d) Quaternary

Last Answer : Primary

Denaturation of proteins involves breakdown of (A) Secondary structure(B) Tertiary structure (C) Quarternary structure(D) All of these

Description : Denaturation of proteins involves breakdown of (A) Secondary structure(B) Tertiary structure (C) Quarternary structure(D) All of these

Last Answer : Answer : D

The hydrogen bonds in the secondary and tertiary structure of proteins are directly attacked by (A) Salts (B) Alkalies (C) Detergents (D) All of these

Description : The hydrogen bonds in the secondary and tertiary structure of proteins are directly attacked by (A) Salts (B) Alkalies (C) Detergents (D) All of these

Last Answer : Answer : B

The primary structure of a protein refers to : (a) whether the protein is fibrous or globular (b) the amino acid sequence in the polypeptide chain (c) the orientation of the amino acid side chains in space (d) the presence or absence of an α-helix

Description : The primary structure of a protein refers to : (a) whether the protein is fibrous or globular (b) the amino acid sequence in the polypeptide chain (c) the orientation of the amino acid side chains in space (d) the presence or absence of an α-helix

Last Answer : the amino acid sequence in the polypeptide chain

Protein present in hemoglobin has the structure known as (A) Primary (B) Secondary (C) Tertiary (D) Quarternary

Description : Protein present in hemoglobin has the structure known as (A) Primary (B) Secondary (C) Tertiary (D) Quarternary

Last Answer : Answer : D

Which are the forces that maintain the second- ary, tertiary and quaternary structures of a pro- tein?

Description : Which are the forces that maintain the second- ary, tertiary and quaternary structures of a pro- tein?

Last Answer : Hydrogen bonds, Electrostatic bonds, Van der Waalís forces and Hydrophobic bonds.

The nucleotide binding site of G-proteins is present on their (A) α-Subunit (B) β-Subunit α- and β- (C) γ-Subunit (D) δ-Subunit

Description : The nucleotide binding site of G-proteins is present on their (A) α-Subunit (B) β-Subunit α- and β- (C) γ-Subunit (D) δ-Subunit

Last Answer : Answer : A

Explain the primary, secondary and tertiary sectors by giving examples of each. -SST 10th

Description : Explain the primary, secondary and tertiary sectors by giving examples of each. -SST 10th

Last Answer : Primary Sector :- All those economic activities that are undertaken by directly using natural resources are included in primary sector. For example, mining, forestry, fishing, poultry etc. Secondary sector : ... to the market. That will be done by tertiary sector. It is also called service sector.

When egg albumin is heated till it is coagulated, the secondary and tertiary structures of the proteins are completely lost resulting in a mixture of randomly arranged (A) Dipeptide chains (B) Tripeptide chains (C) Polypeptide chains(D) All of these

Description : When egg albumin is heated till it is coagulated, the secondary and tertiary structures of the proteins are completely lost resulting in a mixture of randomly arranged (A) Dipeptide chains (B) Tripeptide chains (C) Polypeptide chains(D) All of these

Last Answer : Answer : C

Which of the following structures can polypeptides have? (a) primary structure (b) secondary structure (c) tertiary structure (d) all of the these

Description : Which of the following structures can polypeptides have? (a) primary structure (b) secondary structure (c) tertiary structure (d) all of the these

Last Answer : all of the these

Denaturation refers to the loss of the ______ structure of a ______ molecule. a. primary; carbohydrate b. molecular; fat c. secondary; starch d. tertiary; protein

Description : Denaturation refers to the loss of the ______ structure of a ______ molecule. a. primary; carbohydrate b. molecular; fat c. secondary; starch d. tertiary; protein

Last Answer : d. tertiary; protein

In glucose the orientation of the —H and —OH groups around the carbon atom 5 adjacent to the terminal primary alcohol carbon determines (A) D or L series (B) Dextro or levorotatory (C) α and β anomers (D) Epimers

Description : In glucose the orientation of the —H and —OH groups around the carbon atom 5 adjacent to the terminal primary alcohol carbon determines (A) D or L series (B) Dextro or levorotatory (C) α and β anomers (D) Epimers

Last Answer : A

When haemoglobin takes up oxygen there is a change in the structure due to the moving closer together of (A) β-chains (B) β-chains (C) γ-chains (D) α and γ chains

Description : When haemoglobin takes up oxygen there is a change in the structure due to the moving closer together of (A) β-chains (B) β-chains (C) γ-chains (D) α and γ chains

Last Answer : Answer : A

Which of the following is the “quaternary structure” of proteins concerned with? (a) sequence of amino acids in the peptide chain (b) description of the way the peptide chains are arranged with respect to each other (c) location of the disulfide bridges in the peptide chain (d) conformation of the protein backbone

Description : Which of the following is the quaternary structure of proteins concerned with? (a) sequence of amino acids in the peptide chain (b) description of the way the peptide chains are arranged with ... (c) location of the disulfide bridges in the peptide chain (d) conformation of the protein backbone

Last Answer : description of the way the peptide chains are arranged with respect to each other

Tertiary structure of a protein describes (A) The order of amino acids (B) Location of disulphide bonds (C) Loop regions of proteins (D) The ways of protein folding

Description : Tertiary structure of a protein describes (A) The order of amino acids (B) Location of disulphide bonds (C) Loop regions of proteins (D) The ways of protein folding

Last Answer : Answer : D

The products received by exploiting natural resources come under which one of the following sectors? (a) Quaternary (b) Tertiary

Description : The products received by exploiting natural resources come under which one of the following sectors? (a) Quaternary (b) Tertiary

Last Answer : The products received by exploiting natural resources come under which one of the following sectors? (a) ... b) Tertiary (c) Secondary (d) Primary

Assuming roughly equivalent molecular weights, which of the following would have the highest boiling point? (a) a tertiary amine (b) a quaternary ammonium salt (c) an alcohol (d) an ether

Description : Assuming roughly equivalent molecular weights, which of the following would have the highest boiling point? (a) a tertiary amine (b) a quaternary ammonium salt (c) an alcohol (d) an ether

Last Answer : a quaternary ammonium salt

Which of the following is the main structural feature of proteins? (a) Peptide linkage (b) Ester linkage (c) Ether linkage (d) α,β-Linkage

Description : Which of the following is the main structural feature of proteins? (a) Peptide linkage (b) Ester linkage (c) Ether linkage (d) α,β-Linkage

Last Answer : Peptide linkage

α-helix is stabilized by (A) Hydrogen bonds (B) Disulphide bonds (C) Salt bonds (D) Non-polar bonds

Description : α-helix is stabilized by (A) Hydrogen bonds (B) Disulphide bonds (C) Salt bonds (D) Non-polar bonds

Last Answer : Answer : A

α-helix is disrupted by certain amino acids like (A) Proline (B) Arginine (C) Histidine (D) Lysine

Description : α-helix is disrupted by certain amino acids like (A) Proline (B) Arginine (C) Histidine (D) Lysine

Last Answer : Answer : A

The distance travelled per turn of α-helix in nm is (A) 0.34 (B) 0.44 (C) 0.54 (D) 0.64

Description : The distance travelled per turn of α-helix in nm is (A) 0.34 (B) 0.44 (C) 0.54 (D) 0.64

Last Answer : Answer : C

Each turn of α-helix contains the number of amino acids (A) 2.8 (B) 3.2 (C) 3.4 (D) 3.6

Description : Each turn of α-helix contains the number of amino acids (A) 2.8 (B) 3.2 (C) 3.4 (D) 3.6

Last Answer : Answer : D

α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide bonds

Description : α-Helix is formed by (A) Hydrogen bonds (B) Hydrophobic bonds (C) Electrostatic bonds (D) Disulphide bonds

Last Answer : Answer : A

An amino acid that does not take part in α helix formation is (A) Histidine (B) Tyrosine (C) Proline (D) Tryptophan

Description : An amino acid that does not take part in α helix formation is (A) Histidine (B) Tyrosine (C) Proline (D) Tryptophan

Last Answer : Answer : C

At the lowest energy level α-helix of polypeptide chain is stabilised (A) By hydrogen bonds formed between the H of peptide N and the carbonyl O of the residue (B) Disulphide bonds (C) Non polar bonds (D) Ester bonds

Description : At the lowest energy level α-helix of polypeptide chain is stabilised (A) By hydrogen bonds formed between the H of peptide N and the carbonyl O of the residue (B) Disulphide bonds (C) Non polar bonds (D) Ester bonds

Last Answer : Answer : A

Along the α-helix each amino acid residue advances in nm by (A) 0.15 (B) 0.10 (C) 0.12 (D) 0.20

Description : Along the α-helix each amino acid residue advances in nm by (A) 0.15 (B) 0.10 (C) 0.12 (D) 0.20

Last Answer : Answer : A

Each turn of α-helix contains the amino acid residues (number): (A) 3.6 (B) 3.0 (C) 4.2 (D) 4.5

Description : Each turn of α-helix contains the amino acid residues (number): (A) 3.6 (B) 3.0 (C) 4.2 (D) 4.5

Last Answer : Answer : A

What type of bonding helps in stabilishing the a-helix structure of proteins? -Chemistry

Description : What type of bonding helps in stabilishing the a-helix structure of proteins? -Chemistry

Last Answer : a-helix formation -» Intramolecular hydrogen bonding.

What type of bonding helps in stabilising the -helix structure of proteins ?

Description : What type of bonding helps in stabilising the -helix structure of proteins ?

Last Answer : Ans. In a -helix structure, polypeptide chain of amino acids coils as a right handed screw  because of the formation of all possible Hydrogen bonds between — NH group at each amino residue and > C = 0 group of adjacent turn of helix.

The primary reason for preferring phentolamine as the α adrenergic blocker for performing diagnostic test for pheochromocytoma is: A. It produces rapid and short lasting α-adrenergic blockade B. It equally blocks α1 and α2 adrenoceptors C. It is the most potent α blocker D. It has no additional β adrenergic blocking property

Description : The primary reason for preferring phentolamine as the α adrenergic blocker for performing diagnostic test for pheochromocytoma is: A. It produces rapid and short lasting α-adrenergic blockade B. It equally ... It is the most potent α blocker D. It has no additional β adrenergic blocking property

Last Answer : A. It produces rapid and short lasting α-adrenergic blockade

The primary reason for preferring phentolamine as the α adrenergic blocker for performing diagnostic test for pheochromocytoma is: A. It produces rapid and short lasting α-adrenergic blockade B. It equally blocks α1 and α2 adrenoceptors C. It is the most potent α blocker D. It has no additional β adrenergic blocking property

Description : The primary reason for preferring phentolamine as the α adrenergic blocker for performing diagnostic test for pheochromocytoma is: A. It produces rapid and short lasting α-adrenergic blockade B. It equally ... It is the most potent α blocker D. It has no additional β adrenergic blocking property

Last Answer : A. It produces rapid and short lasting α-adrenergic blockade

The mutarotation of glucose is characterized by : (a) a change from an aldehyde to ketone structure. (b) a change of specific rotation from a (+) to a (–) value. (c) the presence of an intramolecular bridge structure. (d) the irreversible change from α-D to the β-D form.

Description : The mutarotation of glucose is characterized by : (a) a change from an aldehyde to ketone structure. (b) a change of specific rotation from a (+) to a (–) value. (c) the presence of an intramolecular bridge structure. (d) the irreversible change from α-D to the β-D form.

Last Answer : the presence of an intramolecular bridge structure.

All the following statements about epidermal growth factor are true except (A) It is a protein (B) It possess quaternary structure (C) Its receptor is made up of a single polypeptide chain (D) Its receptor possesses tyrosine kinase domain

Description : All the following statements about epidermal growth factor are true except (A) It is a protein (B) It possess quaternary structure (C) Its receptor is made up of a single polypeptide chain (D) Its receptor possesses tyrosine kinase domain

Last Answer : Answer : B

In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds

Description : In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds

Last Answer : Answer : D

What is meant by quaternary structure of a pro- tein?

Description : What is meant by quaternary structure of a pro- tein?

Last Answer : Certain polypeptides will aggregate to form one functional protein. This is referred to as the qua- ternary structure.

What is tertiary structure of proteins? -Biology

Description : What is tertiary structure of proteins? -Biology

Last Answer : Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. ... .[1][2] A number of tertiary structures may fold into a quaternary structure.[3]

What is tertiary structure of proteins? -Biology

Description : What is tertiary structure of proteins? -Biology

Last Answer : answer: