HR BLOCK CERTIFIED PREPARER
PRACTICE EVALUATION 2026 QUESTIONS
WITH ANSWERS GRADED A+
⩥Ramachandran plots. Answer: Φ = N-R
ψ = C-R
optimal angle to prevent steric hinderance
⩥Protein structure of a helix, B sheet, reverse turn. Answer: a:
LEMARKHQ
B: VICYFTW
RT: PSDNG
⩥how many amino acids in alpha turn helix. Answer: 3.6
⩥Super secondary structure. Answer: helix turn helix
⩥parallel vs. antiparallel. Answer: parallel wedges face same way
antiparallel face opposite
⩥Isoelectric point (pI). Answer: pH at which a particular molecule
carries no net electrical charge.
,⩥Protein Separation Techniques (ALL). Answer: Homogenization
Salting Out
Affinity Chromatgraphy
Ion Exchange
Size Exclusion/Gel Filtration
H, S, A, I, SG
He said all individuals SinG
⩥Protein Separation Techniques (H). Answer: Homogenization
disrupt cells, sonicator, centrifuge
⩥Protein Separation Techniques (S). Answer: Salting out
different proteins precipitate out at different salt concentrations
⩥Protein Separation Techniques (A). Answer: Affinity chromatography
add a tag; histidine binds; see how well there is an affinity for the group
⩥Protein Separation Techniques (I). Answer: ion exchange
separation based on charge; + proteins stick to - beads
, ⩥Protein Separation Techniques (SG). Answer: Size Exclusion/Gel
Filtration
separation based on size
⩥Cuts (protein separation techniques). Answer: cut out what dont
need/isnt protein
(use 40% concen. then keep liquid; if use 60% concen. then keep pellet)
⩥Dialysis. Answer: protein separation based on bad with pores
1. Moles in bag + moles in buffer
2. Divide moles by total volume - new concentration
⩥Electrophoresis. Answer: gels - move by size with electric current
1. Isoelectric focusing - purely pH
2. SDS page
pH separation is by pI and charge in 2d
⩥Protein sequencing (who cuts after what). Answer: Cyanogen bromide
= methionine
trypsin = K, and R
chymotrypsin = F, M, L, W, Y
⩥IP. Answer: Immunoprecipitation with proteins
PRACTICE EVALUATION 2026 QUESTIONS
WITH ANSWERS GRADED A+
⩥Ramachandran plots. Answer: Φ = N-R
ψ = C-R
optimal angle to prevent steric hinderance
⩥Protein structure of a helix, B sheet, reverse turn. Answer: a:
LEMARKHQ
B: VICYFTW
RT: PSDNG
⩥how many amino acids in alpha turn helix. Answer: 3.6
⩥Super secondary structure. Answer: helix turn helix
⩥parallel vs. antiparallel. Answer: parallel wedges face same way
antiparallel face opposite
⩥Isoelectric point (pI). Answer: pH at which a particular molecule
carries no net electrical charge.
,⩥Protein Separation Techniques (ALL). Answer: Homogenization
Salting Out
Affinity Chromatgraphy
Ion Exchange
Size Exclusion/Gel Filtration
H, S, A, I, SG
He said all individuals SinG
⩥Protein Separation Techniques (H). Answer: Homogenization
disrupt cells, sonicator, centrifuge
⩥Protein Separation Techniques (S). Answer: Salting out
different proteins precipitate out at different salt concentrations
⩥Protein Separation Techniques (A). Answer: Affinity chromatography
add a tag; histidine binds; see how well there is an affinity for the group
⩥Protein Separation Techniques (I). Answer: ion exchange
separation based on charge; + proteins stick to - beads
, ⩥Protein Separation Techniques (SG). Answer: Size Exclusion/Gel
Filtration
separation based on size
⩥Cuts (protein separation techniques). Answer: cut out what dont
need/isnt protein
(use 40% concen. then keep liquid; if use 60% concen. then keep pellet)
⩥Dialysis. Answer: protein separation based on bad with pores
1. Moles in bag + moles in buffer
2. Divide moles by total volume - new concentration
⩥Electrophoresis. Answer: gels - move by size with electric current
1. Isoelectric focusing - purely pH
2. SDS page
pH separation is by pI and charge in 2d
⩥Protein sequencing (who cuts after what). Answer: Cyanogen bromide
= methionine
trypsin = K, and R
chymotrypsin = F, M, L, W, Y
⩥IP. Answer: Immunoprecipitation with proteins
