High-energy channeling in protein folding
(1997) In Biochemistry 36(25). p.7633-7637- Abstract
- Recent controversy about the role of populated intermediates in protein folding emphasizes the need to better characterize other events on the folding pathway. A complication is that these involve high-energy states which are difficult to target experimentally since they do not accumulate kinetically. Here, we explore the energetics of high-energy states and map out the shape of the free-energy profile for folding of the two-state protein U1A. The analysis is based on nonlinearities in the GdnHCl dependence of the activation energy for unfolding, which we interpret in terms of structural changes of the protein-folding transition state. The result suggests that U1A folds by high-energy channeling where most of the conformational search... (More)
- Recent controversy about the role of populated intermediates in protein folding emphasizes the need to better characterize other events on the folding pathway. A complication is that these involve high-energy states which are difficult to target experimentally since they do not accumulate kinetically. Here, we explore the energetics of high-energy states and map out the shape of the free-energy profile for folding of the two-state protein U1A. The analysis is based on nonlinearities in the GdnHCl dependence of the activation energy for unfolding, which we interpret in terms of structural changes of the protein-folding transition state. The result suggests that U1A folds by high-energy channeling where most of the conformational search takes place isoenergetically at transition-state level. This is manifested in a very broad and flat activation barrier, the top of which covers more than 60% of the reaction coordinate. The interpretation favors a folding mechanism where the pathway leading to the native protein is determined by the sequence's ability to stabilize productive transition (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/127109
- author
- Silow, Maria and Oliveberg, Mikael LU
- organization
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- CHYMOTRYPSIN INHIBITOR-2, KINETIC-ANALYSIS, NUCLEATION-CONDENSATION MECHANISM, TRANSITION-STATE, BINDING, DENATURATION, BEHAVIOR, DOMAIN
- in
- Biochemistry
- volume
- 36
- issue
- 25
- pages
- 7633 - 7637
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:0030750236
- pmid:9201903
- ISSN
- 0006-2960
- DOI
- 10.1021/bi970210x
- language
- English
- LU publication?
- yes
- id
- 22e4c2cd-a8b9-4c2a-bbf5-b47c19cd08fc (old id 127109)
- date added to LUP
- 2016-04-01 12:31:18
- date last changed
- 2022-01-27 06:10:58
@article{22e4c2cd-a8b9-4c2a-bbf5-b47c19cd08fc,
abstract = {{Recent controversy about the role of populated intermediates in protein folding emphasizes the need to better characterize other events on the folding pathway. A complication is that these involve high-energy states which are difficult to target experimentally since they do not accumulate kinetically. Here, we explore the energetics of high-energy states and map out the shape of the free-energy profile for folding of the two-state protein U1A. The analysis is based on nonlinearities in the GdnHCl dependence of the activation energy for unfolding, which we interpret in terms of structural changes of the protein-folding transition state. The result suggests that U1A folds by high-energy channeling where most of the conformational search takes place isoenergetically at transition-state level. This is manifested in a very broad and flat activation barrier, the top of which covers more than 60% of the reaction coordinate. The interpretation favors a folding mechanism where the pathway leading to the native protein is determined by the sequence's ability to stabilize productive transition}},
author = {{Silow, Maria and Oliveberg, Mikael}},
issn = {{0006-2960}},
keywords = {{CHYMOTRYPSIN INHIBITOR-2; KINETIC-ANALYSIS; NUCLEATION-CONDENSATION MECHANISM; TRANSITION-STATE; BINDING; DENATURATION; BEHAVIOR; DOMAIN}},
language = {{eng}},
number = {{25}},
pages = {{7633--7637}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Biochemistry}},
title = {{High-energy channeling in protein folding}},
url = {{http://dx.doi.org/10.1021/bi970210x}},
doi = {{10.1021/bi970210x}},
volume = {{36}},
year = {{1997}},
}