BIOMG 3300 Unit 3 Objectives Questions with Correct Answers.
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Course
BIOMG 3300
Institution
BIOMG 3300
BIOMG 3300 Unit 3 Objectives Questions with Correct Answers.
Fe3+ - Correct Answer doesn't allow for reversible binding to O2
Fe2+ when bound to 2 heme groups - Correct Answer can cause the formation of radicals, which are bad for the body
Ligand - Correct Answer a molecule reversibly bound ...
BIOMG 3300 Unit 3 Objectives Questions with Correct
Answers.
Fe3+ - Correct Answer doesn't allow for reversible binding to O2
Fe2+ when bound to 2 heme groups - Correct Answer can cause the formation of radicals, which are
bad for the body
Ligand - Correct Answer a molecule reversibly bound by a protein
binding site - Correct Answer the place where a ligand binds to a protein complementary in
size/charge/shape/hydrophilic/hydrophobic character
induced fit - Correct Answer structural adaptation that occurs between ligand and protein
substrate - Correct Answer a molecule acted on by an enzyme
catalytic/active site - Correct Answer ligand binding site on an enzyme
myoglobin - Correct Answer a protein used for oxygen storage in muscle
-very high affinity for O2, not sensitive to changes in [O2]
-hyperbolic affinity curve
-1 subunit, no cooperativity
heme group - Correct Answer a prosthetic group bound to a protein that incorporates and sequesters
free Fe
Pyrrole ring - Correct Answer the actual unit of porphyrin ring (in heme groups)
Order of AAs most likely to be in protein interior - Correct Answer 1) hydrophobic AAs
2) charged AAs
3) polar uncharged AAs
, Fe has how many coordination points - Correct Answer 6: 4 bound to porphyrin ring, 1 bound to
proximal His, 1 is O2 binding site
Globin - Correct Answer a family of proteins with similar 2' and 3' structures, used for oxygen
storage. Most have 8 alpha helices and have heme nestled between 2 of them with 2 His residues
coordinated to it
P50 - Correct Answer the PO2 where half of the molecule is bound to O2 (50% protein saturation)
proximal His role - Correct Answer Keeps Fe in heme group as Fe2+ by binding to coordination bond
distal His role - Correct Answer -increases heme's affinity for O2 by forming an H bond with
it/stabilizing it
-decreases bound Hb's affinity for CO
-guards access to heme pocket, can rotate quickly to allow it in molecular breathing
How do Globin prevent Fe oxidation - Correct Answer sequester the Fe deep into the protein, and
make sure that the proximal His occupies 6th coordination bond
molecular breathing - Correct Answer molecular motions-eg rapid flexing of side chains- in a
molecule, needed to allow O2 to enter/leave heme pocket in myoglobin
Hemoglobin - Correct Answer a tetramic protein with 2 alpha and 2 beta globin side chains
-less O2 affinity than myoglobin, influenced by [O2]
-4 subunits, cooperative binding
What interactions are in hemoglobin 4' structure? - Correct Answer hydrophobic effect, H bonds, ion
pairs/salt bridges between unlike subunits
1' sequence in myoglobin and hemoglobin - Correct Answer not similar
3' structure of hemoglobin 1 subunit to myoglobin - Correct Answer quite similar, same alpha helix
naming ocnventions
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