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

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
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Answer : D
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Folding of newly synthesized proteins is accelerated by (A) Protein disulphide isomerase (B) Prolyl cis-trans isomerase (C) Chaperonins (D) All of these

Description : Folding of newly synthesized proteins is accelerated by (A) Protein disulphide isomerase (B) Prolyl cis-trans isomerase (C) Chaperonins (D) All of these

Last Answer : Answer : D

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

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

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

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

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 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

Many globular proteins are stable in solution although they lack in (A) Hydrogen bonds (B) Salt bonds (C) Non-polar bonds (D) Disulphide bonds

Description : Many globular proteins are stable in solution although they lack in (A) Hydrogen bonds (B) Salt bonds (C) Non-polar bonds (D) Disulphide bonds

Last Answer : Answer : D

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

Many globular proteins are stable in solution inspite they lack in (A) Disulphide bonds (B) Hydrogen bonds (C) Salt bonds (D) Non polar bonds

Description : Many globular proteins are stable in solution inspite they lack in (A) Disulphide bonds (B) Hydrogen bonds (C) Salt bonds (D) Non polar bonds

Last Answer : Answer : A

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

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

Which of the following is the first step in the determination of the primary structure of proteins? (a) determining the number and kind of amino acids in the peptide (b) reducing the disulfide bridges in the protein (c) protecting the N-terminal of the peptide (d) protecting the C-terminal of the peptide

Description : Which of the following is the first step in the determination of the primary structure of proteins? (a) determining the number and kind of amino acids in the peptide (b) reducing the disulfide bridges ... (c) protecting the N-terminal of the peptide (d) protecting the C-terminal of the peptide

Last Answer : reducing the disulfide bridges in the protein

Digestion of protein-is necessary because (a)It not absorbed as such (b)Proteins are large molecules. (c) Proteins have complex structure. (d) Proteins are made of amino acids

Description : Digestion of protein-is necessary because (a)It not absorbed as such (b)Proteins are large molecules. (c) Proteins have complex structure. (d) Proteins are made of amino acids

Last Answer : (a)It not absorbed as such

Hydrophobic bonds are formed in protein be- tween which amino acids?

Description : Hydrophobic bonds are formed in protein be- tween which amino acids?

Last Answer : Valine, leucine and isoleucine residues. 

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

Tertiary protein structure ionic bonds -Biology

Description : Tertiary protein structure ionic bonds -Biology

Last Answer : answer:

Amino acid sequence directs protein folding?

Description : Insulin possesses two polypeptide chains denoted A and B that are linked by disulfide bonds. Upon denaturation by reduction of the SH groups of insulin, followed by reoxidation, only 7% of the ... can these data be reconciled with the hypothesis that the amino acid sequence directs protein folding?

Last Answer : Insulin is synthesized as preproinsulin that is proteolytically processed in the β cells of the islets of Langerhans in the pancreas, to give proinsulin. After synthesis and folding, a section of the ... lacking the C peptide, lacks some of the information necessary to direct the folding process. 

Which of the following is the least likely to be involved in stabilising the three-dimensional folding of most proteins(a) Hydrogen bonds (b) Electrostatic interaction (c) Hydrophobic interaction (d) Ester bonds

Description : Which of the following is the least likely to be involved in stabilising the three-dimensional folding of most proteins (a) Hydrogen bonds (b) Electrostatic interaction (c) Hydrophobic interaction (d) Ester bonds

Last Answer : (d) Ester bonds

What happens at the ribosome in the production of a protein? a. mRNA brings the codon b. tRNA brings the anticodon c. the amino acids are linked by polypeptide bonds d. translation e. all the above

Description : What happens at the ribosome in the production of a protein? a. mRNA brings the codon b. tRNA brings the anticodon c. the amino acids are linked by polypeptide bonds d. translation e. all the above

Last Answer : c. the amino acids are linked by polypeptide bonds

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

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

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

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

Last Answer : Answer : B

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

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 number of intra-chain disulphide bonds in pro-insulin: (A) One (B) Two (C) Three (D) Four

Description : The number of intra-chain disulphide bonds in pro-insulin: (A) One (B) Two (C) Three (D) Four

Last Answer : Answer : C

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

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

Which of the following statement(s) is/are true concerning protein/amino acid metabolism in man? a. The major source of amino acids is breakdown of circulating proteins b. The recommended daily allowance for protein may triple in critically ill patients c. Urinary nitrogen losses will approach 0 in the face of protein starvation d. Negative nitrogen balance refers to a decrease in nitrogen taken into the body versus the amount of nitrogen lost

Description : Which of the following statement(s) is/are true concerning protein/amino acid metabolism in man? a. The major source of amino acids is breakdown of circulating proteins b. The recommended daily ... balance refers to a decrease in nitrogen taken into the body versus the amount of nitrogen lost

Last Answer : Answer: b, d About 15% of the total body weight is made up of proteins, about half of which are intracellular and half extracellular. In man and other animals, dietary protein is the source of ... is exceeded by the amount of nitrogen lost in the urine, stool, skin, wounds, and fistula drainage

A characteristic of protein synthesis in both the archaea and eukarya is A.transcription and translation are coupled B.translation is inhibited by diphtheria toxin C.proteins are synthesized from D-, rather than L-, isomers of amino acids D.the initiator tRNA is charged with N-formyl- methionine

Description : A characteristic of protein synthesis in both the archaea and eukarya is A.transcription and translation are coupled B.translation is inhibited by diphtheria toxin C.proteins are synthesized from D-, ... L-, isomers of amino acids D.the initiator tRNA is charged with N-formyl- methionine

Last Answer : C.proteins are synthesized from

A characteristic of protein synthesis in both the archaea and eukarya is A- transcription and translation are coupled B- translation is inhibited by diphtheria toxin C- .proteins are synthesized from D-, rather than L-, isomers of amino acids D- the initiator tRNA is charged with N-formyl-methionine

Description : A characteristic of protein synthesis in both the archaea and eukarya is A- transcription and translation are coupled B- translation is inhibited by diphtheria toxin C- .proteins are synthesized from D-, rather than L-, isomers of amino acids D- the initiator tRNA is charged with N-formyl-methionine

Last Answer : .proteins are synthesized from D-, rather than L-, isomers of amino acids

Which statement about hormone types is correct? A) Non-steroid hormones activate an enzyme cascade. B) Steroid hormones regulate the production of a particular protein. C) Non-steroid hormones are either amino acids, peptides, or proteins. D) Steroid hormones all have four carbon rings with different side chains. E) All of the choices are correct.

Description : Which statement about hormone types is correct? A) Non-steroid hormones activate an enzyme cascade. B) Steroid hormones regulate the production of a particular protein. C) Non-steroid hormones are ... all have four carbon rings with different side chains. E) All of the choices are correct.

Last Answer : E) All of the choices are correct.

Dolichol phosphate is A- a complex lipid involved in docking vesicles with the plasma membrane B- the anchor on which sugars assemble before transfer to proteins C- a chaperone used in protein folding D- a product of phospholipase C activation

Description : Dolichol phosphate is A- a complex lipid involved in docking vesicles with the plasma membrane B- the anchor on which sugars assemble before transfer to proteins C- a chaperone used in protein folding D- a product of phospholipase C activation

Last Answer : the anchor on which sugars assemble before transfer to proteins

Agonists affect the receptor molecule in the following manner: A. Alter its amino acid sequence B. Denature the receptor protein C. Alter its folding or alignment of subunits D. Induce covalent bond formation

Description : Agonists affect the receptor molecule in the following manner: A. Alter its amino acid sequence B. Denature the receptor protein C. Alter its folding or alignment of subunits D. Induce covalent bond formation

Last Answer : C. Alter its folding or alignment of subunits

Agonists affect the receptor molecule in the following manner: A. Alter its amino acid sequence B. Denature the receptor protein C. Alter its folding or alignment of subunits D. Induce covalent bond formation

Description : Agonists affect the receptor molecule in the following manner: A. Alter its amino acid sequence B. Denature the receptor protein C. Alter its folding or alignment of subunits D. Induce covalent bond formation

Last Answer : C. Alter its folding or alignment of subunits

The active site of an enzyme is formed by (A) R group of amino acids (B) NH2 group of amino acids (C) CO group of amino acids (D) Sulphur bonds which are exposed

Description : The active site of an enzyme is formed by (A) R group of amino acids (B) NH2 group of amino acids (C) CO group of amino acids (D) Sulphur bonds which are exposed

Last Answer : Answer : A

The active site of an enzyme is formed by a few of the enzymes: (A) R groups of the amino acids (B) Amino groups of the amino acids (C) Carboxyl group of the amino acids (D) Exposed sulfur bonds

Description : The active site of an enzyme is formed by a few of the enzymes: (A) R groups of the amino acids (B) Amino groups of the amino acids (C) Carboxyl group of the amino acids (D) Exposed sulfur bonds

Last Answer : Answer : C

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

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

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

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

What is meant by tertiary structure of a protein?

Description : What is meant by tertiary structure of a protein?

Last Answer : The tertiary structure denotes three dimensional structure of the whole protein. It defines the steric relationship of amino acids which are far apart from each other in the linear sequence.

In denaturation of proteins, the bond which is not broken: (A) Disulphide bond (B) Peptide bond (C) Hydrogen bond (D) Ionic bond

Description : In denaturation of proteins, the bond which is not broken: (A) Disulphide bond (B) Peptide bond (C) Hydrogen bond (D) Ionic bond

Last Answer : Answer : B

An amino acid which contains a disulphide bond is (A) Lysine (B) Methionine (C) Homocysteine (D) Cystine

Description : An amino acid which contains a disulphide bond is (A) Lysine (B) Methionine (C) Homocysteine (D) Cystine

Last Answer : Answer : D

The primary structure of a protein refers to the sequence of amino acids that are linked together in a long chain. Which of the following common items would best represent the primary structure of a protein?

Description : The primary structure of a protein refers to the sequence of amino acids that are linked together in a long chain. Which of the following common items would best represent the primary structure of a protein?

Last Answer : beads of different colors joined together on a piece of string

What level of protein structure is affected by substituting charged amino acids with non polar ones?

Description : What level of protein structure is affected by substituting charged amino acids with non polar ones?

Last Answer : Feel Free to Answer

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

Stem and loop structures are A- proteins that help partially denatured enzymes to recover their native configuration B- structures in DNA caused by inverted repeats C- structures at the ends of linear eukaryotic DNA molecules D- the bonds between adjacent DNA nucleotides in the same strand

Description : Stem and loop structures are A- proteins that help partially denatured enzymes to recover their native configuration B- structures in DNA caused by inverted repeats C- structures at the ends of linear eukaryotic DNA molecules D- the bonds between adjacent DNA nucleotides in the same strand

Last Answer : structures in DNA caused by inverted repeats