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Home
‣
Biochemistry
‣
Protein Stability
Comments
Question
Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of
Options
A. 1-3 other amino acids
B. 5-7 other amino acids
C. 9-12 other amino acids
D. 13-15 other amino acids
Correct Answer
5-7 other amino acids
Protein Stability problems
Search Results
1. The correlation between free energy ?G transfer between the aqueous/organic phases and the surface area of amino acid residues
Options
A. reflects the reduction in solvent-accessible area during protein folding
B. is only meaningful for the polar amino acids
C. ignores the important contribution of the peptide bond
D. is similar to effects seen with SDS denaturation
Show Answer
Scratch Pad
Discuss
Correct Answer: reflects the reduction in solvent-accessible area during protein folding
2. For the unfolding reaction of Protein G, ∆H° =210.6 kJ/mol, this means that
Options
A. unfolding is favored enthalpically
B. folding is favored enthalpically
C. the entropy is positive at all temperatures
D. the entropy is negative at all temperatures
Show Answer
Scratch Pad
Discuss
Correct Answer: folding is favored enthalpically
3. Which of the three subunits of the G proteins binds GDP and GTP?
Options
A. Alpha
B. Beta
C. Gamma
D. Delta
Show Answer
Scratch Pad
Discuss
Correct Answer: Alpha
4. The heme is held in place by a bond between
Options
A. the Fe
2+
and cysteine
B. the Fe
3+
and histidine
C. the Fe
3+
and cysteine
D. the Fe
2+
and histidine
Show Answer
Scratch Pad
Discuss
Correct Answer: the Fe
2+
and histidine
5. The major element of secondary structure in myoglobin and hemoglobin is
Options
A. the P-strand
B. the a-helix
C. the reverse turn
D. All of these
Show Answer
Scratch Pad
Discuss
Correct Answer: the a-helix
6. Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein
Options
A. only at the ends of a-helices
B. only at the turns connecting p-strands
C. only on Pro residues
D. rarely
Show Answer
Scratch Pad
Discuss
Correct Answer: rarely
7. Since ?G° = -RTlnK
Options
A. a 10-fold increase in K decreases ?G° by about 10-fold
B. a 10-fold decrease in K decreases ?G° by about 2.3*RT
C. a 10-fold increase in K decreases ?G° by about 2.3*RT
D. a 10-fold decrease in K increases ?G° by about 10-fold
Show Answer
Scratch Pad
Discuss
Correct Answer: a 10-fold increase in K decreases ?G° by about 2.3*RT
8. At the midpoint of a temperature transition curve,
Options
A. half of the protein is denatured
B. K
eq
= 1.0 and ?G = 0
C. [Native] = [Unfolded]
D. All of these
Show Answer
Scratch Pad
Discuss
Correct Answer: All of these
9. Which of the following is the most correct?
Options
A. Charged amino acids are never buried in the interior of a protein
B. Charged amino acids are seldom buried in the interior of a protein
C. All hydrophobic amino acids are buried when a protein folds
D. Tyrosine is only found in the interior of proteins
Show Answer
Scratch Pad
Discuss
Correct Answer: Charged amino acids are seldom buried in the interior of a protein
10. Which of the following forces is the most unfavorable for protein folding?
Options
A. Conformational entropy
B. Hydrophobic interactions
C. Vander Waals interactions
D. Electrostatic interactions
Show Answer
Scratch Pad
Discuss
Correct Answer: Conformational entropy
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Amino Acid Metabolism
Anti Bodies
Antigen
ATP Synthesis and Fatty Acid Oxidation
Carbohydrate
Cell Signalling and Transduction
Cell Structure and Compartments
Chromatography
Disease Associated with Immune System
DNA Structure and Replication
Enzymes
FT IR Spectroscopy
Gas Chromatography
Gel Electrophoresis
Genetic Code and Regulation
Genetic Regulation Prokaryotes
Glycolysis
HPLC
Immune Response
Immune System
Immunological Techniques
Lipid
Membrane Structure and Functions
Minerals
Nitrogen Metabolism
NMR Spectroscopy
Nucleic Acids
Oxidative Phosphorylation
Photosynthesis and Respiration
Polymerase Chain Reaction
Protein and Nucleic Acid Interactions
Protein Purification
Protein Stability
Protein Structure
Protein Synthesis
Recombinant DNA Technology
RNA Structure
Spectroscopy
Structure and Properties of Amino Acids
Structure and Properties of Peptides
TCA Cycle
Thermodynamics and Free Energy
Transcription and Regulation
UV Luminance Spectroscopy
Vitamins and Coenzymes
Water, pH and Macromolecules