View Single Post
  #1  
Unread 11-25-2010, 08:21 PM
nmrlearner's Avatar
nmrlearner nmrlearner is offline
Senior Member
 
Join Date: Jan 2005
Posts: 23,134
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 0
Downloads: 0
Uploads: 0
Default An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mu

An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.

Related Articles An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.

J Am Chem Soc. 2005 Apr 13;127(14):5066-72

Authors: Choy WY, Zhou Z, Bai Y, Kay LE

15N relaxation dispersion NMR spectroscopy has been used to study exchange dynamics in a pair of mutants of Rd-apocyt b562, a redesigned four-helix-bundle protein. An analysis of the relaxation data over a range of temperatures establishes that exchange in both proteins is best modeled as two-state and that it derives from the folding/unfolding transition. These results are in accord with predictions based on the reaction coordinate for the folding of the protein determined from native-state hydrogen exchange data [Chu, R.; Pei, W.; Takei, J.; Bai, Y. Biochemistry 2002, 41, 7998-8003]. The kinetics and thermodynamics of the folding transition have been characterized in detail. Although only a narrow range of temperatures could be examined, it is clear that the folding rate temperature profile is distinctly non-Arrhenius for both mutants, with the folding barrier for at least one of them entropic.

PMID: 15810841 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No