The stability of a protein's folded conformation is primarily determined by all of the following EXCEPT:
Hydrophobic interactions
Hydrogen bonds
Disulfide bonds
Glycosidic bonds
Related Questions
A protein undergoes denaturation in a high urea concentration. Which of the following interactions is LEAST likely to be disrupted during this process?
Hydrophobic interactions
Hydrogen bonds
Ionic interactions
Peptide bonds
What type of bonds primarily stabilize the secondary structure of a protein?
Peptide bonds
Disulfide bonds
Hydrogen bonds
Hydrophobic interactions
Which of the following is the least likely to be involved in stabilizing the three-dimensional folding of most proteins?
Hydrophobic interactions
Hydrogen bonds
Disulfide bonds
Van der Waals forces
Which chromatographic technique is BEST suited for separating proteins based on their differences in net charge at a given pH?
Size exclusion chromatography
Affinity chromatography
Ion exchange chromatography
Hydrophobic interaction chromatography
A novel protein was discovered containing a unique amino acid with a side chain composed of a selenol group (-SeH). Compared to a cysteine residue (-SH) in a similar protein, this selenol-containing amino acid would MOST likely exhibit which property?
Increased reactivity towards oxidizing agents
Decreased reactivity towards oxidizing agents
Identical reactivity towards oxidizing agents
Formation of stronger disulfide bonds
Which statement correctly describes the N-terminal of a polypeptide chain?
It has a free amino group.
It has a free carboxyl group.
It represents the first amino acid in the chain.
It is involved in the formation of peptide bonds with other amino acids.
The globular proteins undergo structural changes, in response to extremes of pH or temperature, the process called
Renaturation
Denaturation
Combination
Both (a) and (b)
Richest source of protein is
Rice
Gram
Wheat
Glycine max
Which of the following is the least likely to be involved in stabilizing the three-dimensional folding of most proteins?
Ester bonds
Hydrogen bonds
Electrostatic interaction
Hydrophobic interaction
Basic structure of proteins was given by
Linus Pauling and Robert Corey
Emil Fischer
Frederick Sanger
James Watson and Francis Crick