Biochemistry ACS Final Exam
Questions and Answers 100%
PASS
What is the Henderson-Hasselbach ?—ANSWER-pH = pka + log ([A]/[Ha])
High Ka, low pka indicates what?—ANSWER-Strong acid
What is the relation between pH and [H+]?—ANSWER-pH = -log[H+]
What is the realtionship between pka and Ka?—ANSWER-pka = -logKa
What makes a good buffer?—ANSWER-A weak acid mixed with its conjugate
base in a 50/50 ratio
What destroys tryptophan?—ANSWER-Acids and bases
What is the isoelectric point?—ANSWER-The pH in which a particular
molecule carries no net charge (pI)
Side chain pka of aspartic acid?—ANSWER-~ 3.86
Side chain pka of arginine?—ANSWER-~ 12.48
Side chain pka of cysteine?—ANSWER-~8.0
Side chain pka of glutamic acid?—ANSWER-~4.07
Side chain pka of histidine?—ANSWER-~6.1
, Side chain pka of lysine?—ANSWER-~10.53
Side chain pka of tyrosine?—ANSWER-~10.00
Inductive effect on pka?—ANSWER-Electronegative atoms pull electrons
away from another group, and makes that particular groups more positive.
Generally lowers pka
Electrostatic effect on pka?—ANSWER-Nearby positive charge makes a
proton want to leave more, generally lowers pka.
Distance effect on pka?—ANSWER-Generally lowers the influence of
inductive and electrostatic effects
How are amino acids read?—ANSWER-N terminus to C terminus
How to find specific activity?—ANSWER-mols of pdt / min / mg of protein
What does specific activity measure?—ANSWER-It measures the purity of
the protein
What happens near a protein's isoelectric point?—ANSWER-The protein
loses solubility
How to separate proteins by size (all or none)?—ANSWER-1. Filtration
2. Dialysis
How to separate proteins by size (little by little)?—ANSWER-SDS page; runs
negative to positive after interaction with SDS; migration related to log of
molecular weight; largest move least
© 2026 Copyright. All Rights Reserved. This document is
protected by copyright law
Questions and Answers 100%
PASS
What is the Henderson-Hasselbach ?—ANSWER-pH = pka + log ([A]/[Ha])
High Ka, low pka indicates what?—ANSWER-Strong acid
What is the relation between pH and [H+]?—ANSWER-pH = -log[H+]
What is the realtionship between pka and Ka?—ANSWER-pka = -logKa
What makes a good buffer?—ANSWER-A weak acid mixed with its conjugate
base in a 50/50 ratio
What destroys tryptophan?—ANSWER-Acids and bases
What is the isoelectric point?—ANSWER-The pH in which a particular
molecule carries no net charge (pI)
Side chain pka of aspartic acid?—ANSWER-~ 3.86
Side chain pka of arginine?—ANSWER-~ 12.48
Side chain pka of cysteine?—ANSWER-~8.0
Side chain pka of glutamic acid?—ANSWER-~4.07
Side chain pka of histidine?—ANSWER-~6.1
, Side chain pka of lysine?—ANSWER-~10.53
Side chain pka of tyrosine?—ANSWER-~10.00
Inductive effect on pka?—ANSWER-Electronegative atoms pull electrons
away from another group, and makes that particular groups more positive.
Generally lowers pka
Electrostatic effect on pka?—ANSWER-Nearby positive charge makes a
proton want to leave more, generally lowers pka.
Distance effect on pka?—ANSWER-Generally lowers the influence of
inductive and electrostatic effects
How are amino acids read?—ANSWER-N terminus to C terminus
How to find specific activity?—ANSWER-mols of pdt / min / mg of protein
What does specific activity measure?—ANSWER-It measures the purity of
the protein
What happens near a protein's isoelectric point?—ANSWER-The protein
loses solubility
How to separate proteins by size (all or none)?—ANSWER-1. Filtration
2. Dialysis
How to separate proteins by size (little by little)?—ANSWER-SDS page; runs
negative to positive after interaction with SDS; migration related to log of
molecular weight; largest move least
© 2026 Copyright. All Rights Reserved. This document is
protected by copyright law
