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ACS Biochemistry Final Exam: Questions & Solutions
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ACS Biochemistry Final Exam: Questions & Solutions
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ACS Biochemistry Final Exam: Questions & SolutionspKa (chapter 3) Right Ans - measure of the tendency of a group to give up a
proton (acidity); tendency decreases tenfold as pKa increases by one unit
thioester bond (1) Right Ans - compounds with functional group C-S-CoA-C
(eg, in acetyl-CoA)
zwitterion (3) Right Ans - dipolar ion with both positive and negative
groups but overall neutral charge; can act as either an acid or base
Isoelectric point (pI) (chapter 3) Right Ans - the characteristic pH at which
the net electric charge is zero
SDS - Sodium Dodecyl Sulfate (chap 3) Right Ans - detergent used to unfold
proteins and give them uniform negative charge
SDS Page (3) Right Ans - chromatography used to separate proteins based
on mass. light proteins travel fast than heavier ones
PCR - Polymerase chain reaction (3) Right Ans - copies DNA multiple times
to increase sample size
Isoelectric focusing (chapt 3) Right Ans - procedure used to determine the
isoelectric pt (pI) of a protein. Protein migrates through gel until pH = pI (net
charge = 0)
Two-Dimensional Electrophoresis (3) Right Ans - combines isoelectric
focusing and SDS electrophoresis; separates proteins by both molecular
weight and pI
specific activity (3) Right Ans - number of enzyme units per mg of total
protein (a measure of enzyme purity)
activity (3) Right Ans - total units of a certain enzyme in a solution
Peptide bonds (chapter 4) Right Ans - C-N bond with double bond
character due to resonance (C-N bond cannot rotate, and is planar)
, Edman degredation (3) Right Ans - used in the sequencing of polypeptides;
labels and removes ONLY the amino-residue from a polypeptide. carried out
in a machine called a sequenator
φ in peptide bonding (chapter 4) Right Ans - angle around the α-carbon -
amide nitrogen bond
ψ in peptide bonding (chapter 4) Right Ans - angle around the α-carbon -
carbonyl carbon bond
Ramachandran Plot (4) Right Ans - shows favoreable φ- ψ angle
combinations. 3 main "wells" for α-helices, β-sheets, and left handed α-helices
Levinthal's Paradox (4) Right Ans - protein folding cannot be a completely
random, trial and error process
chaperonins (4) Right Ans - elaborite protein complexes required for the
folding of a number of cellular proteins that do not fold spontaneously
Henderson-Hasselbach Equation (2) Right Ans - pH = pKa + log([A-]/[HA])
which amino acids are not found in α-helices? (4) Right Ans - glycine and
proline. glycine is too flexible, proline is too rigid to rotate.
which amino acids are commonly found in β turns? (4) Right Ans - glycine,
because it is small and flexible, and proline because it forms cis conformation
in tight turns.
β-mercaptoethanol (4) Right Ans - breaks disulfide bonds
circular dichroism (4) Right Ans - technique that measures the amount of
helical structures in macromolecule (protein is denatured)
Acid Dissasociation constant Ka (2) Right Ans - quantitative measure of the
strength of an acid in solution
Native Fold Right Ans -
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