This title appears in the Scientific Report :
2006
Please use the identifier:
http://dx.doi.org/10.1529/biophysj.106.087668 in citations.
Please use the identifier: http://hdl.handle.net/2128/2373 in citations.
Folding of proteins with diverse folds
Folding of proteins with diverse folds
Using parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold. In all three cases, simulations with our en...
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Personal Name(s): | Mohanty, S. |
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Hansmann, U. H. E. | |
Contributing Institute: |
John von Neumann - Institut für Computing; NIC |
Published in: | Biophysical journal, 91 (2006) S. 3537 |
Imprint: |
New York, NY
Rockefeller Univ. Press
2006
|
Physical Description: |
3537 |
PubMed ID: |
16950845 |
DOI: |
10.1529/biophysj.106.087668 |
Document Type: |
Journal Article |
Research Program: |
Scientific Computing |
Series Title: |
Biophysical Journal
92 |
Subject (ZB): | |
Link: |
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Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/2373 in citations.
Using parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold. In all three cases, simulations with our energy function find the native structures as global minima in free energy at experimentally relevant temperatures. However, the folding process strongly differs for the three molecules, indicating that the folding mechanism is correlated with the form of the native structure. |