Ninhydrin reaction gives a purple colour and evolves CO2 with (A) Peptide bonds (B) Histamine (C) Ergothioneine (D) Aspargine

Ninhydrin reaction gives a purple colour and evolves CO2 with (A) Peptide bonds (B) Histamine (C) Ergothioneine (D) Aspargine
by

1 Answer

Answer :

Answer : D
by
selected

Related questions

Ninhydrin with evolution of CO2 forms a blue complex with (A) Peptide bond (B) α-Amino acids (C) Serotonin (D) Histamine

Description : Ninhydrin with evolution of CO2 forms a blue complex with (A) Peptide bond (B) α-Amino acids (C) Serotonin (D) Histamine

Last Answer : Answer : B

The amino acid which gives yellow colour with Ninhydrin in paper chromatography is (A) Tyrosine (B) Proline (C) Tryptophan (D) Alanine

Description : The amino acid which gives yellow colour with Ninhydrin in paper chromatography is (A) Tyrosine (B) Proline (C) Tryptophan (D) Alanine

Last Answer : Answer : B

Edman’s reaction can be used to (A) Determine the number of tyrosine residues in a protein (B) Determine the number of aromatic amino acid residues in a protein (C) Determine the amino acid sequence of a protein (D) Hydrolyse the peptide bonds in a protein

Description : Edman’s reaction can be used to (A) Determine the number of tyrosine residues in a protein (B) Determine the number of aromatic amino acid residues in a protein (C) Determine the amino acid sequence of a protein (D) Hydrolyse the peptide bonds in a protein

Last Answer : Answer : C

Which of the following gives a positive Ninhydrin test? (A) Reducing sugar (B) Triglycerides (C) α-amino acids (D) Phospholipids

Description : Which of the following gives a positive Ninhydrin test? (A) Reducing sugar (B) Triglycerides (C) α-amino acids (D) Phospholipids

Last Answer : Answer : C

Which of the followings gives a positive test for Ninhydrin? (A) Reducing sugars (B) Triglycerides (C) Alpha aminoacids (D) Esterified Fats

Description : Which of the followings gives a positive test for Ninhydrin? (A) Reducing sugars (B) Triglycerides (C) Alpha aminoacids (D) Esterified Fats

Last Answer : Answer : C

What is the importance of ninhydrin reaction?

Description : What is the importance of ninhydrin reaction?

Last Answer : It is used for qualitative test and quantitative es- timation of amino acids. It is often used for detec- tion of amino acids in chromatography.

What is ninhydrin reaction?

Description : What is ninhydrin reaction?

Last Answer : All amino acids when heated with ninhydrin will give a pink colour.

The formation of a peptide bond during the elongation step of protein synthesis results in the splitting of how many high energy bonds? (A) 1 (B) 2 (C) 3 (D) 4

Description : The formation of a peptide bond during the elongation step of protein synthesis results in the splitting of how many high energy bonds? (A) 1 (B) 2 (C) 3 (D) 4

Last Answer : Answer : B

The chemical forces that bind most coenzymes and substrates to enzymes such as LDH are (A) Hydrogen bonds (B) Peptide bonds (C) Coordinate bonds (D) Covalent bonds

Description : The chemical forces that bind most coenzymes and substrates to enzymes such as LDH are (A) Hydrogen bonds (B) Peptide bonds (C) Coordinate bonds (D) Covalent bonds

Last Answer : Answer : D

A protein reacts with biuret reagent which indicates 2 or more (A) Blood clotting (B) Peptide bond (C) Disulphide bonds (D) Hydrophobic bonds

Description : A protein reacts with biuret reagent which indicates 2 or more (A) Blood clotting (B) Peptide bond (C) Disulphide bonds (D) Hydrophobic bonds

Last Answer : Answer : B

The bond in proteins that is not broken under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds

Description : The bond in proteins that is not broken under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds

Last Answer : Answer : D

The hydrogen bonds between peptide linkages are interfered by (A) Guanidine (B) Uric acid (C) Salicylic acid (D) Oxalic acid

Description : The hydrogen bonds between peptide linkages are interfered by (A) Guanidine (B) Uric acid (C) Salicylic acid (D) Oxalic acid

Last Answer : Answer : A

A coiled structure in which peptide bonds are folded in regular manner by (A) Globular proteins (B) Fibrous proteins (C) Both (A) and (B) (D) None of these

Description : A coiled structure in which peptide bonds are folded in regular manner by (A) Globular proteins (B) Fibrous proteins (C) Both (A) and (B) (D) None of these

Last Answer : Answer : A

Proteins react with biuret reagent which is suggestive of 2 or more (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) Hydrophobic bonds

Description : Proteins react with biuret reagent which is suggestive of 2 or more (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) Hydrophobic bonds

Last Answer : Answer : B

The bond in proteins that is not hydrolysed under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds

Description : The bond in proteins that is not hydrolysed under usual conditions of denaturation: (A) Hydrophobic bond (B) Hydrogen bond (C) Disulphide bond (D) Peptide bonds

Last Answer : Answer : C

Bonds that are formed between two cysteine residues is (A) Disulphide (B) Peptide (C) Electrostatic (D) Hydrophobic

Description : Bonds that are formed between two cysteine residues is (A) Disulphide (B) Peptide (C) Electrostatic (D) Hydrophobic

Last Answer : Answer : A

The only correct statement about chymotrypsin is (A) It is formed from trypsin (B) Carboxypeptidase converts trypsin into chymotrypsin (C) Its optimum pH is around 7 (D) It hydrolyses peptide bonds involving basic amino acids

Description : The only correct statement about chymotrypsin is (A) It is formed from trypsin (B) Carboxypeptidase converts trypsin into chymotrypsin (C) Its optimum pH is around 7 (D) It hydrolyses peptide bonds involving basic amino acids

Last Answer : Answer : C

All the following statements about pepsin are correct except (A) It is smaller than pepsinogen (B) It is formed by the action of HCl on its precursor (C) Its optimum pH is 1.0–2.0 (D) It hydrolyses the C-terminal and N-terminal peptide bonds of proteins

Description : All the following statements about pepsin are correct except (A) It is smaller than pepsinogen (B) It is formed by the action of HCl on its precursor (C) Its optimum pH is 1.0–2.0 (D) It hydrolyses the C-terminal and N-terminal peptide bonds of proteins

Last Answer : Answer : D

Primary structure of a protein is formed by (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) All of these

Description : Primary structure of a protein is formed by (A) Hydrogen bonds (B) Peptide bonds (C) Disulphide bonds (D) All of these

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

Chymotrypsin is specific for peptide bonds containing (A) Uncharged amino acid residues (B) Acidic amino acids (C) Basic amino acid (D) Small amino acid residues

Description : Chymotrypsin is specific for peptide bonds containing (A) Uncharged amino acid residues (B) Acidic amino acids (C) Basic amino acid (D) Small amino acid residues

Last Answer : Answer : A

The enzyme trypsin is specific for peptide bonds of (A) Basic amino acids (B) Acidic amino acids (C) Aromatic amino acids (D) Next to small amino acid residues

Description : The enzyme trypsin is specific for peptide bonds of (A) Basic amino acids (B) Acidic amino acids (C) Aromatic amino acids (D) Next to small amino acid residues

Last Answer : Answer : A

Denaturation of proteins results in (A) Disruption of primary structure (B) Breakdown of peptide bonds (C) Destruction of hydrogen bonds (D) Irreversible changes in the molecule

Description : Denaturation of proteins results in (A) Disruption of primary structure (B) Breakdown of peptide bonds (C) Destruction of hydrogen bonds (D) Irreversible changes in the molecule

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

The hydrogen bonds between peptide linkages of a protein molecules are interfered by (A) Guanidine (B) Uric acid (C) Oxalic acid (D) Salicylic acid

Description : The hydrogen bonds between peptide linkages of a protein molecules are interfered by (A) Guanidine (B) Uric acid (C) Oxalic acid (D) Salicylic acid

Last Answer : Answer : A

How many peptide bonds are present in a trip- eptide?

Description : How many peptide bonds are present in a trip- eptide?

Last Answer :  A tripeptide is a combination of three amino ac- ids; so there are two peptide bonds.

All amino acids have one asymmetric carbon atom, except (A) Arginine (B) Aspargine (C) Histidine (D) Glycine

Description : All amino acids have one asymmetric carbon atom, except (A) Arginine (B) Aspargine (C) Histidine (D) Glycine

Last Answer : Answer : D

The amino acid which has a pK near 4 and thus is negatively charged at pH 7 is (A) Alanine (B) Glutamic acid (C) Glutamine (D) Aspargine

Description : The amino acid which has a pK near 4 and thus is negatively charged at pH 7 is (A) Alanine (B) Glutamic acid (C) Glutamine (D) Aspargine

Last Answer : Answer : B

The amino acids in which the R groups have a net positive charge at pH 7.0 are (A) Lysine, Arginine, Histidine (B) Lysine, Aspargine (C) Histidine, Aspargine (D) Glutamine, Arginine

Description : The amino acids in which the R groups have a net positive charge at pH 7.0 are (A) Lysine, Arginine, Histidine (B) Lysine, Aspargine (C) Histidine, Aspargine (D) Glutamine, Arginine

Last Answer : Answer : A

The acid amide of Aspartic acid is (A) Glutamine (B) Arginine (C) Aspargine (D) Ornithine

Description : The acid amide of Aspartic acid is (A) Glutamine (B) Arginine (C) Aspargine (D) Ornithine

Last Answer : Answer : C

Which among the following is a basic amino acid? (A) Aspargine (B) Arginine (C) Proline (D) Alanine

Description : Which among the following is a basic amino acid? (A) Aspargine (B) Arginine (C) Proline (D) Alanine

Last Answer : Answer : B

Which compound gives both ninhydrin test and Molisch’s test? -Do You Know?

Description : Which compound gives both ninhydrin test and Molisch’s test? -Do You Know?

Last Answer : answer:

A compound gives a positive Tollens' test but negative Ninhydrin test. It is (a) a protein (b) an amino acid (c) a monosaccharide (d) pyridine

Description : A compound gives a positive Tollens' test but negative Ninhydrin test. It is (a) a protein (b) an amino acid (c) a monosaccharide (d) pyridine

Last Answer : a monosaccharide

Which compound gives both ninhydrin test and Molisch's test?

Description : Which compound gives both ninhydrin test and Molisch's test?

Last Answer : protein

In nitroprusside test, amino acid cysteine produces a: (A) Red colour (B) Blue colour (C) Yellow colour (D) Purple colour

Description : In nitroprusside test, amino acid cysteine produces a: (A) Red colour (B) Blue colour (C) Yellow colour (D) Purple colour

Last Answer : Answer : A

In Nitroprusside test, amino acid cystein produces (A) Blue colour complex (B) Red colour (C) Yellow colour (D) Purple colour

Description : In Nitroprusside test, amino acid cystein produces (A) Blue colour complex (B) Red colour (C) Yellow colour (D) Purple colour

Last Answer : Answer : B

What are the Reaction of amino acid using ninhydrin and biuret reagent?

Description : What are the Reaction of amino acid using ninhydrin and biuret reagent?

Last Answer : What is the answer ?

Digestion of proteins involves (a) changes in secondary structure only (b) cleavage of peptide linkages (c) removal of all carboxyl groups in the form of CO2. (d) removal of all NH2 groups in the form of NH3

Description : Digestion of proteins involves (a) changes in secondary structure only (b) cleavage of peptide linkages (c) removal of all carboxyl groups in the form of CO2. (d) removal of all NH2 groups in the form of NH3

Last Answer : cleavage of peptide linkages

The useful reagent for detection of amino acids is (A) Molisch reagent (B) Dichlorophenol Indophenol (C) Ninhydrin (D) Biuret

Description : The useful reagent for detection of amino acids is (A) Molisch reagent (B) Dichlorophenol Indophenol (C) Ninhydrin (D) Biuret

Last Answer : Answer : C

Sanger’s reagent contains (A) Phenylisothiocyanate (B) Dansyl chloride (C) 1-Fluoro-2, 4-dinitrobenzene (D) Ninhydrin

Description : Sanger’s reagent contains (A) Phenylisothiocyanate (B) Dansyl chloride (C) 1-Fluoro-2, 4-dinitrobenzene (D) Ninhydrin

Last Answer : Answer : C

Primary structure of proteins can be determined by the use of (A) Electrophoresis (B) Chromatography (C) Ninhydrin (D) Sanger’s reagent

Description : Primary structure of proteins can be determined by the use of (A) Electrophoresis (B) Chromatography (C) Ninhydrin (D) Sanger’s reagent

Last Answer : Answer : D

Do proteins give a color with ninhydrin?

Description : Do proteins give a color with ninhydrin?

Last Answer : Proteins do not give a true color reaction; but N- terminal end amino group of protein will react with ninhydrin, to produce a blue color.

How peptide bonds are formed? -Biology

Description : How peptide bonds are formed? -Biology

Last Answer : answer:

When all the peptide bonds of a protein have been broken down . The result would be

Description : When all the peptide bonds of a protein have been broken down . The result would be

Last Answer : When all the peptide bonds of a protein have been broken down . The result would be A. Amide B. Oligosaccharide C. Polypeptide D. Amino acid

What organelles form peptide bonds between amino acids?

Description : What organelles form peptide bonds between amino acids?

Last Answer : Ribosomes. They are constructed from protein themselves, but, more germane to the question, they are also partially composed of catalytic RNA, which forges the peptide bonds.

What Peptide bonds form between the?

Description : What Peptide bonds form between the?

Last Answer : What is the answer ?

What organelles form peptide bonds between amino acids?

Description : What organelles form peptide bonds between amino acids?

Last Answer : Ribosomes. They are constructed from protein themselves, but, more germane to the question, they are also partially composed of catalytic RNA, which forges the peptide bonds.

A chain of amino acids joined by peptide bonds is called as (a) Peptide chain (b) Polypeptide chain (c) Polyamino acid chain (d) Nucleotide chain

Description : A chain of amino acids joined by peptide bonds is called as (a) Peptide chain (b) Polypeptide chain (c) Polyamino acid chain (d) Nucleotide chain

Last Answer : Ans. ((b))

Enzymes contain 1. Peptide bonds 2. Amino acids 3. Halogens 4. Fatty acids The correct answers are: (a) 1 and 4 (b) 1,3 and 4 (c) 1 and 2 (d) 2, 3 and 4

Description : Enzymes contain 1. Peptide bonds 2. Amino acids 3. Halogens 4. Fatty acids The correct answers are: (a) 1 and 4 (b) 1,3 and 4 (c) 1 and 2 (d) 2, 3 and 4

Last Answer : Ans:(c)

The two strands of the DNA double helix are held together by (a) Hydrogen bonds (b)C=C double bonds (c) Hydrophobic bonds (d) Peptide bonds

Description : The two strands of the DNA double helix are held together by (a) Hydrogen bonds (b)C=C double bonds (c) Hydrophobic bonds (d) Peptide bonds

Last Answer : Ans:(a)