ACS BIOCHEMISTRY STUDY
MATERIAL 2026 TESTED QUESTIONS
AND ACCURATE SOLUTIONS
◉ Reacts with the N-terminus of the protein to produce a 2,4-
dinitrophenol derivative that labels the first residue. Can repeat
hydrolysis to determine sequential amino acids
Answer: FDNB
◉ Reduces disulfide bonds.
Answer: DTT
◉ Adds carboxymethyl group on free -SH groups. Blocks disulfide
bonding.
Answer: Iodoacetate
◉ Bonds between two -SH groups that form between 2° and 3°
structure.
Answer: Disulfide-bonds
◉ Breaks disulfide bonds.
Answer: ßME
◉ Formed from 2 α-helices twisted around each other. "Coiled coil".
Cross-linked by disulfide bonds.
,Answer: α-keratin
◉ Repeating sequence of Gly-X-Pro. 3 stranded "coiled coil". Contains
gly core.
Answer: Collagen
◉ Less distinct areas of α and ß folding.
Answer: α/ß Protein Folding
◉ Two distinct areas of α and ß folding.
Answer: α+ß Protein Folding
◉ Electrons in Fe are "spread out" and result in larger atom.
Answer: High-Spin Fe
◉ Electrons are less "spread out" and are compacted by electron rich
porphyrin ring.
Answer: Low-Spin Fe
◉ Heme is in high-spin state. H2O is bound to heme.
Answer: T-State
◉ Heme is in low-spin state. O2 is bound to heme.
Answer: R-State
, ◉ Greatly reduces hemoglobin's affinity for O2 by binding
allosterically.
Answer: BPG
◉ Slope of Lineweaver-Burke Graph
Answer: Km/Vmax
◉ Y-intercept of Lineweaver-Burke Graph
Answer: 1/Vmax
◉ X-intercept of Linewaever-Burke Graph
Answer: -1/Km
◉ Kcat
Answer: Vmax/Et
◉ Slope of Competitive Inhibition
Answer: αKm/Vmax
◉ X-intercept of Competitive Inhibition
Answer: -1/αKm
MATERIAL 2026 TESTED QUESTIONS
AND ACCURATE SOLUTIONS
◉ Reacts with the N-terminus of the protein to produce a 2,4-
dinitrophenol derivative that labels the first residue. Can repeat
hydrolysis to determine sequential amino acids
Answer: FDNB
◉ Reduces disulfide bonds.
Answer: DTT
◉ Adds carboxymethyl group on free -SH groups. Blocks disulfide
bonding.
Answer: Iodoacetate
◉ Bonds between two -SH groups that form between 2° and 3°
structure.
Answer: Disulfide-bonds
◉ Breaks disulfide bonds.
Answer: ßME
◉ Formed from 2 α-helices twisted around each other. "Coiled coil".
Cross-linked by disulfide bonds.
,Answer: α-keratin
◉ Repeating sequence of Gly-X-Pro. 3 stranded "coiled coil". Contains
gly core.
Answer: Collagen
◉ Less distinct areas of α and ß folding.
Answer: α/ß Protein Folding
◉ Two distinct areas of α and ß folding.
Answer: α+ß Protein Folding
◉ Electrons in Fe are "spread out" and result in larger atom.
Answer: High-Spin Fe
◉ Electrons are less "spread out" and are compacted by electron rich
porphyrin ring.
Answer: Low-Spin Fe
◉ Heme is in high-spin state. H2O is bound to heme.
Answer: T-State
◉ Heme is in low-spin state. O2 is bound to heme.
Answer: R-State
, ◉ Greatly reduces hemoglobin's affinity for O2 by binding
allosterically.
Answer: BPG
◉ Slope of Lineweaver-Burke Graph
Answer: Km/Vmax
◉ Y-intercept of Lineweaver-Burke Graph
Answer: 1/Vmax
◉ X-intercept of Linewaever-Burke Graph
Answer: -1/Km
◉ Kcat
Answer: Vmax/Et
◉ Slope of Competitive Inhibition
Answer: αKm/Vmax
◉ X-intercept of Competitive Inhibition
Answer: -1/αKm
