Home⇒ Medical Science⇒ Biochemistry⇒ Protein stability
| 1-Dont try to cram or spend more time here just read it fast and cover syllabus then practice MCQ's cheptor of same topic to check your progress. . |
| 2-Wrong options are also given but dont concentrate there, Right answer is in bold format. |
| Q1 ⇒ Attractive Vander Waals forces occur between any pair of nearby atoms [other wrong options] [Discuss in forum] |
| Q2 ⇒ Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein rarely [other wrong options] [Discuss in forum] |
| Q3 ⇒ If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? The primary structure of ovalbumin [other wrong options] [Discuss in forum] |
| Q4 ⇒ Which of the following forces is the most unfavorable for protein folding? Conformational entropy [other wrong options] [Discuss in forum] |
| Q5 ⇒ For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that folding is favored enthalpically [other wrong options] [Discuss in forum] |
| Q6 ⇒ Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 5-7 other amino acids [other wrong options] [Discuss in forum] |
| Q7 ⇒ At the midpoint of a temperature transition curve, All of these [other wrong options] [Discuss in forum] |
| Q8 ⇒ The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues reflects the reduction in solvent-accessible area during protein folding [other wrong options] [Discuss in forum] |
| Q9 ⇒ Which of the following forces is the most favorable for protein folding? Hydrophobic Interactions [other wrong options] [Discuss in forum] |
| Q10 ⇒ Since ΔG° = -RTlnK a 10-fold increase in K decreases ΔG° by about 2.3*RT [other wrong options] [Discuss in forum] |
| Q11 ⇒ Which of the following is the most correct? Charged amino acids are seldom buried in the interior of a protein [other wrong options] [Discuss in forum] |