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:
https://lup.lub.lu.se/record/125440
- author
- Ternström, Tomas
LU
; Mayor, Ugo
; Akke, Mikael
LU
and Oliveberg, Mikael
- organization
- publishing date
- 1999
- 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 Academy of 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
- 2016-04-01 12:14:52
- date last changed
- 2022-01-27 01:00:50
@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}},
keywords = {{Biophysics}},
language = {{eng}},
number = {{26}},
pages = {{14854--14859}},
publisher = {{National Academy of 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}},
url = {{http://www.pnas.org/cgi/content/abstract/96/26/14854}},
volume = {{96}},
year = {{1999}},
}