The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
(1999) In Nature Structural Biology 6(6). p.594-601- Abstract
- The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1114284
- author
- Kragelund, B B ; Osmark, Peter LU ; Neergaard, T B ; Schiodt, J ; Kristiansen, K ; Knudsen, J and Poulsen, F M
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nature Structural Biology
- volume
- 6
- issue
- 6
- pages
- 594 - 601
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:10360367
- scopus:0033015989
- ISSN
- 1072-8368
- DOI
- 10.1038/9384
- language
- English
- LU publication?
- no
- id
- 1fff2182-fa32-4be4-a44d-05b43cebcd5a (old id 1114284)
- date added to LUP
- 2016-04-01 17:12:47
- date last changed
- 2022-01-29 01:11:42
@article{1fff2182-fa32-4be4-a44d-05b43cebcd5a, abstract = {{The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.}}, author = {{Kragelund, B B and Osmark, Peter and Neergaard, T B and Schiodt, J and Kristiansen, K and Knudsen, J and Poulsen, F M}}, issn = {{1072-8368}}, language = {{eng}}, number = {{6}}, pages = {{594--601}}, publisher = {{Nature Publishing Group}}, series = {{Nature Structural Biology}}, title = {{The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP}}, url = {{http://dx.doi.org/10.1038/9384}}, doi = {{10.1038/9384}}, volume = {{6}}, year = {{1999}}, }