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BCH 370 Exam 3 Practice Questions With 100% ALL SURE ANSWERS

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  • Course
  • Biochemistry
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  • Biochemistry

BCH 370 Exam 3 Practice Questions With 100% ALL SURE ANSWERS

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  • September 19, 2024
  • 12
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
  • Biochemistry
  • Biochemistry
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BCH 370 Exam 3 Practice Questions With 100% ALL SURE ANSWERS


Terms in this set (74)

Kd= [P][L]/[PL]
State a definition of Kd using an equation
Kd= [L] when [P]=[PL]

State a definition of Kd in words the amount of free ligand when half of the total protein is bound with ligand




a protein with multiple binding sites, the binding at one site increases the binding affinity at other
Provide a definition of positive cooperativity
sites

a protein with multiple binding sites, the binding at one site decreases the binding affinity at other
Provide a definition of negative cooperativity
sites

a protein with multiple binding sites, the binding at one site does not affect binding affinity at
other sites
Provide a definition of no cooperativity

*only condition that allows for hyperbolic binding curve

Does a large value of Kd indicate tight binding of No, a large value of Kd indicates weak binding of a ligand
a ligand?


BCH 370stand
What does the ITC abbreviation Exam
for? 3 Practiceisothermal
Questions
titration calorimetry


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, The ligand gets added to the inhibitor.
In a typical ITC experiment involving an enzyme
The amount of electrical energy added to the sample to keep the sample the same temperature
and inhibitor, what gets added to what? What gets
as the reference is measured.
measured? What can be learned?
The Kd of ligand binding and thermodynamic parameters can be learned.

In an ITC experiment, why does the amount of As the titration progresses, there are fewer sites available to bind the ligand (because most of the
heat released upon mixing tend to decrease as sites already have bound ligand)
the titration progresses? In other words, why is
less heat released during the last mixing events, Past a certain concentration, adding more ligand has no effect
compared to the first few mixing events?

Which of these can be determined in an ITC all of these can be found by ITC
experiment: deltaH for ligand binding, deltaS,
deltaG, Keq for ligand binding, Kd for ligand
binding.

What are the axis and typical units for a trace from x-axis: time in min or sec
an ITC experiment? y-axis: energy/time in microjoule/sec

Why does the area of each peak in the ITC trace fewer ligand binding sites are available for binding ligand
become smaller as the experiment proceeds?




Differential scanning calorimetry measures the amount of excess electrical energy required to
What is measured in a DSC experiment? What can keep the sample chamber and reference chamber the same temperature. DSC identifies the
be learned? temperatures at which a molecule undergoes structural transitions (or denatures). DSC identifies
the energy associated with each structural transition.

x-axis: temperature
What does a typical DSC curve look like for a y-axis: amount of excess energy transferred to sample
protein that denatures at 60 degrees celsius?
the curve will have a peak at 60 degrees __/\__

Many proteins unfold in a "cooperative" manner. when one part of the protein loses structure, the whole protein unfolds rapidly
What is the meaning of "cooperative" when in the
context of protein unfolding? in other words, a part of the protein can not be unfolded without disrupting the whole structure

An surface plasmon resonance apparatus contains a thin gold film on the surface and glass
Describe an SPR apparatus. Where is the prism.
immobilized protein located? Where is the ligand
located? Immobilized proteins are located and bound on the gold film. Ligand is located in solution on
BCH 370 Exam 3 PracticeoneQuestions
side of the gold surface.

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