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From Snapshot to Movie: φ Analysis of Protein Folding Transition States Taken One Step Further

Ternström, Tomas LU ; Mayor, Ugo; Akke, Mikael LU and Oliveberg, Mikael (1999) In Proceedings of the National Academy of Sciences 96(26). p.14854-14859
Abstract
Kinetic anomalies in protein folding can result from changes of the kinetic ground states (D, I, and N), changes of the protein folding transition state, or both. The 102-residue protein U1A has a symmetrically curved chevron plot which seems to result mainly from changes of the transition state. At low concentrations of denaturant the transition state occurs early in the folding reaction, whereas at high denaturant concentration it moves close to the native structure. In this study we use this movement to follow continuously the formation and growth of U1A's folding nucleus by φ analysis. Although U1A's transition state structure is generally delocalized and displays a typical nucleation-condensation pattern, we can still resolve a... (More)
Kinetic anomalies in protein folding can result from changes of the kinetic ground states (D, I, and N), changes of the protein folding transition state, or both. The 102-residue protein U1A has a symmetrically curved chevron plot which seems to result mainly from changes of the transition state. At low concentrations of denaturant the transition state occurs early in the folding reaction, whereas at high denaturant concentration it moves close to the native structure. In this study we use this movement to follow continuously the formation and growth of U1A's folding nucleus by φ analysis. Although U1A's transition state structure is generally delocalized and displays a typical nucleation-condensation pattern, we can still resolve a sequence of folding events. However, these events are sufficiently coupled to start almost simultaneously throughout the transition state structure. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Biophysics
in
Proceedings of the National Academy of Sciences
volume
96
issue
26
pages
14854 - 14859
publisher
National Acad Sciences
external identifiers
  • scopus:0033592876
ISSN
1091-6490
language
English
LU publication?
yes
id
077dac73-ec53-4991-9301-811eefb1c321 (old id 125440)
alternative location
http://www.pnas.org/cgi/content/abstract/96/26/14854
date added to LUP
2007-07-06 17:11:08
date last changed
2017-02-05 03:39:26
@article{077dac73-ec53-4991-9301-811eefb1c321,
  abstract     = {Kinetic anomalies in protein folding can result from changes of the kinetic ground states (D, I, and N), changes of the protein folding transition state, or both. The 102-residue protein U1A has a symmetrically curved chevron plot which seems to result mainly from changes of the transition state. At low concentrations of denaturant the transition state occurs early in the folding reaction, whereas at high denaturant concentration it moves close to the native structure. In this study we use this movement to follow continuously the formation and growth of U1A's folding nucleus by φ analysis. Although U1A's transition state structure is generally delocalized and displays a typical nucleation-condensation pattern, we can still resolve a sequence of folding events. However, these events are sufficiently coupled to start almost simultaneously throughout the transition state structure.},
  author       = {Ternström, Tomas and Mayor, Ugo and Akke, Mikael and Oliveberg, Mikael},
  issn         = {1091-6490},
  keyword      = {Biophysics},
  language     = {eng},
  number       = {26},
  pages        = {14854--14859},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {From Snapshot to Movie: φ Analysis of Protein Folding Transition States Taken One Step Further},
  volume       = {96},
  year         = {1999},
}