Thread: NMR paper Following protein folding in real time using NMR spectroscopy.
View Single Post
  #1  
Unread 08-22-2010, 03:50 AM
nmrlearner's Avatar
nmrlearner nmrlearner is offline
Senior Member
  
Join Date: Jan 2005
Posts: 23,185
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 Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.

Related Articles Following protein folding in real time using NMR spectroscopy.

Nat Struct Biol. 1995 Oct;2(10):865-70

Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM

The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative manner from an intermediate formed in the dead-time of the experiments. The kinetics of folding to the native state are closely similar to those observed by stopped-flow fluorescence and near-UV circular dichroism. The NMR spectrum of the transient intermediate resembles closely that of the well characterized stable molten globule state formed at low pH. The results suggest that NMR can play a key role in describing at an atomic level the structural transitions occurring during protein folding.

PMID: 7552710 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote

Did you find this post helpful? Yes | No