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Which statement is true about protein folding? ○ The equilibrium between folded and unfolded states is best determined by measuring the time course of unfolding ○ Refolding of a protein typically exhibits a linear dependence on the concentration of denaturant ○ The sigmoidal shape of the unfolding transition reflects the complex architecture of proteins ○ Proteins with stable folding intermediates usually exhibit smooth free-energy funnels ○ The rate of unfolding increases as the temperature increases towards the Tm value

Which statement is true about protein folding? ○ The equilibrium between folded and unfolded states is best determined by measuring the time course of unfolding ○ Refolding of a protein typically exhibits a linear dependence on the concentration of denaturant ○ The sigmoidal shape of the unfolding transition reflects the complex architecture of proteins ○ Proteins with stable folding intermediates usually exhibit smooth free-energy funnels ○ The rate of unfolding increases as the temperature increases towards the Tm value

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Which statement is true about protein folding? ○ The equilibrium between folded and unfolded states is best determined by measuring the time course of unfolding ○ Refolding of a protein typically exhibits a linear dependence on the concentration of denaturant ○ The sigmoidal shape of the unfolding transition reflects the complex architecture of proteins ○ Proteins with stable folding intermediates usually exhibit smooth free-energy funnels ○ The rate of unfolding increases as the temperature increases towards the Tm value
Transcribed Image Text:Which statement is true about protein folding? ○ The equilibrium between folded and unfolded states is best determined by measuring the time course of unfolding ○ Refolding of a protein typically exhibits a linear dependence on the concentration of denaturant ○ The sigmoidal shape of the unfolding transition reflects the complex architecture of proteins ○ Proteins with stable folding intermediates usually exhibit smooth free-energy funnels ○ The rate of unfolding increases as the temperature increases towards the Tm value
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