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BMSC 200 FINAL EXAM QUESTIONS AND ANSWERS

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BMSC 200 FINAL EXAM QUESTIONS AND ANSWERS a ______ binds at a specific site on the protein called the ___________ - answer- ligand, binding site the binding of a ligand may cause __________ in the protein - answer- a conformational change the amount of oxygen can ________ - answer- limit an organisms size oxygen is poorly soluble in ______ - answer- aqueous solutions myoglobin - answer- monomeric protein hemoglobin - answer- tetrameric protein myoglobin is an example of ______ - answer- tertiary structure hemoglobin is an example of ________ - answer- quaternary structure _______ has a higher affinity for oxygen - answer- myoglobin Heme consists of _______ - answer- a photo porphyrin ring bound to a single Fe+2 atom ________ uses heme to enable O2 binding - answer- myoglobin and hemoglobin Fe+2 seeks 6 coordinating interactions: - answer- 4 with heme, 1 with imidazole, and 1 is free for O2 bonding CO has ______ greater affinity than O2 to hemoglobin - answer- 200x myoglobin with 1 heme group can bind ________ - answer- 1 oxygen molecule hemoglobin with 4 hem groups can bind ________ - answer- 4 oxygen molecules myoglobin has _______ for oxygen binding - answer- hyperbolic curve (only one curve) hemoglobin has ______ for oxygen binding - answer- sigmoidal behaviour x axis of O2 binding curve - answer- partial pressure O2 y axis of O2 binding curve - answer- fraction saturation of O2 of the protein the p50 of myoglobin is - answer- 3 torr Hemoglobin is found in_______ - answer- red blood cells hemoglobin is an ______ protein - answer- allosteric allosteric proteins - answer- can adopt 2 different conformations T state - answer- inactive, releases O2 to pheriphery R state - answer- active, higher affinity for O2, saturates O2 in the lungs proteins with _____ cannot achieve a cooperative effect - answer- single ligand binding site allosteric effectors (modulators) - answer- bind allosteric proteins at specific sites allosteric activators - answer- stabilize the R state allosteric inhibitors - answer- stabilize the T state when the ligand and the modulator are the same the interaction is _______ - answer- homotropic when the ligand and the modulator are different the interaction is _____ - answer- heterotropic Example of homotropic activator - answer- oxygen example of heterotropic inhibitor - answer- 2,3 BPG when ligand binding induces a conformation it is called ________ - answer- induced fit the P50 for hemoglobin is - answer- 30 torr hemoglobin works as both - answer- a sensor and responder to hypoxia 2,3 BPG - answer- decreases hemoglobins affinity for oxygen Adaptation to high altitude - answer- increased 2,3 BPG decreases Hb's O2 affinity The bohr effect - answer- at decreased pH Hb has a lower affinity for O2 increased muscle activity - answer- lowers pH Bohr effect - answer- releases oxygen to active tissues How CO2 is transported in the blood - answer- CO2 is taken into red blood cells and converted to bicarbonate and a proton, the proton decreases the pH and more O2 is produced

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BMSC 200 FINAL EXAM QUESTIONS
AND ANSWERS
a ______ binds at a specific site on the protein called the ___________ - answer-
ligand, binding site

the binding of a ligand may cause __________ in the protein - answer- a
conformational change

the amount of oxygen can ________ - answer- limit an organisms size

oxygen is poorly soluble in ______ - answer- aqueous solutions

myoglobin - answer- monomeric protein

hemoglobin - answer- tetrameric protein

myoglobin is an example of ______ - answer- tertiary structure

hemoglobin is an example of ________ - answer- quaternary structure

_______ has a higher affinity for oxygen - answer- myoglobin

Heme consists of _______ - answer- a photo porphyrin ring bound to a single Fe+2
atom

________ uses heme to enable O2 binding - answer- myoglobin and hemoglobin

Fe+2 seeks 6 coordinating interactions: - answer- 4 with heme, 1 with imidazole, and
1 is free for O2 bonding

CO has ______ greater affinity than O2 to hemoglobin - answer- 200x

myoglobin with 1 heme group can bind ________ - answer- 1 oxygen molecule

hemoglobin with 4 hem groups can bind ________ - answer- 4 oxygen molecules

myoglobin has _______ for oxygen binding - answer- hyperbolic curve (only one
curve)

hemoglobin has ______ for oxygen binding - answer- sigmoidal behaviour

x axis of O2 binding curve - answer- partial pressure O2

y axis of O2 binding curve - answer- fraction saturation of O2 of the protein

the p50 of myoglobin is - answer- 3 torr

,Hemoglobin is found in_______ - answer- red blood cells

hemoglobin is an ______ protein - answer- allosteric

allosteric proteins - answer- can adopt 2 different conformations

T state - answer- inactive, releases O2 to pheriphery

R state - answer- active, higher affinity for O2, saturates O2 in the lungs

proteins with _____ cannot achieve a cooperative effect - answer- single ligand
binding site

allosteric effectors (modulators) - answer- bind allosteric proteins at specific sites

allosteric activators - answer- stabilize the R state

allosteric inhibitors - answer- stabilize the T state

when the ligand and the modulator are the same the interaction is _______ -
answer- homotropic

when the ligand and the modulator are different the interaction is _____ - answer-
heterotropic

Example of homotropic activator - answer- oxygen

example of heterotropic inhibitor - answer- 2,3 BPG

when ligand binding induces a conformation it is called ________ - answer- induced
fit

the P50 for hemoglobin is - answer- 30 torr

hemoglobin works as both - answer- a sensor and responder to hypoxia

2,3 BPG - answer- decreases hemoglobins affinity for oxygen

Adaptation to high altitude - answer- increased 2,3 BPG decreases Hb's O2 affinity

The bohr effect - answer- at decreased pH Hb has a lower affinity for O2

increased muscle activity - answer- lowers pH

Bohr effect - answer- releases oxygen to active tissues

How CO2 is transported in the blood - answer- CO2 is taken into red blood cells and
converted to bicarbonate and a proton, the proton decreases the pH and more O2 is
produced

, sickle cell anemia - answer- results from a single amino acid change (Glu6Val)

in SCA the cells in T state - answer- link together to form fibres

SCA red blood cells act as - answer- a plug which blocks blood flow

hemocyanin - answer- uses copper to bind oxygen

hemocyanin has no ______ - answer- heme group

hemocyanin is not localized within - answer- specialized oxygen transport cells

membranes are built from - answer- amphapathic molecules

membranes are impermeable to - answer- polar molecules

liposomes act as - answer- a vesicle for delivery through membranes

membranes are primarily made up of - answer- lipids and protiens

most active membranes have a higher ratio of - answer- protein to lipid

proteins and lipids move across the membrane - answer- laterally, rapidly

flippases - answer- enzymes that catalyze the transfer of lipids from one side of the
bilayer to the other

lipid raft - answer- a group of lipids that float together as a unit within a larger sea of
lipids

lipid rafts arise from - answer- spontaneous association of lipid molecules whose
tails are similar lengths

apoptosis - answer- cell destruction

peripheral membrane proteins - answer- associated with membrane through
electrostatic or hydrogen bonding interactions

bulk of peripheral proteins are found in - answer- cytosol or extracellular space

lipid anchored membrane protein - answer- can anchor proteins to the membrane,
post translational modification

GI anchored proteins are always found on - answer- outer face

Integral membrane protiens - answer- are immersed in the span of the membrane

side chains within the transmembrane region are nonpolar except for - answer-
carbonyl and amide groups

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