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Which forces stabilize the quaternary structures of proteins?
Hydrophobic effect, Ionic Bonding, Hydrogen Bonding, van der Walls forces, and Disulfide Bonding.
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Where does F1-ATPase exist?
Mitochondria
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What is the function of F1-ATPase?
Responsible for generationg ATP from ADP in mitochondria.
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What is an amphipathic alpha-helix?
Contains hydroPHOBIC residues on one side of the chain and hydroPHILIC residues on the other side.
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When 2 or more amphipathic alpha-helices associate along their long axis, they form...
A coiled coil.
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The interior of BILOGICAL membranes are composed of __________ fatty acid chains.
hydrophobic
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What are the 3 dynamic properties of proteins?
Atomic Fluctuations, Collective Motions (breathing), and Triggered Conformational Changes.
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What are the transmembrain proteins that form conducting pores through the lipid bilayer of cells?
Ion Channels
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What is an environmentally-induced fluctuation in the struction and function of ion channel proteions called?
Gating
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What is a stimulated, long-range structural alteration that leads to functional changes in a proteins properties called?
Allostery
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Channels undergo allosteric changes to convert between conducting and nonconducting states. What is this?
Gating
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What is it when ion channels open to conduct ions?
Activation
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What is it when ion channels close to block conduction?
Deactivation
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What is it when ion conduction is blocked rapidly following channel activation?
Inactivation
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What is an apo-conformation?
An unbound state.
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____________ only happens when Neurotransmitter-gated ion channels open and close after a receptor is excited for a "long" period of time.
Desensitization
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What is the Michaelis-Menten equation?
V/Vmax = s/s+Km
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A protein that has little or no enzymatic activity; but once it is processed posttranslationally, it become competent for catalysis.
Zymogen or Proenzyme
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The small group of catalytic RNAs that can catalyze chemical reactions.
Ribozymes
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An organic, non-peptidicmolecule that needs to bind an enzyme so that the enzyme can catalyze a chemical reaction.
Coenzymes or Cofactors
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The term ________________ imples that the coenzyme is tightly or covalently bound to the enzyme and does not dissociate from the enzyme during catalysis.
prosthetic groups
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A coenzyme-dependent enzyme that does not have a coenzyme bound to it and needs something to work properly.
Apoenzyme
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An enzyme that has its coenzyme tightly bound to it.
Holoenzyme
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Enzymes that catalyze the same reaction yet differ in their amino acid sequence.
Isozyme (isoenzyme)
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A _____________ starts with the binding of substrate and ends with the release of product and formation of the enzyme in its initial state, for instance.
catalytic cycle
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One ___________ is usually the amount of enzyme that produced 1 umol of product per minute.
enzyme unit (U)
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As Km goes up, [substrate] _______.
goes up, as well
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