This title appears in the Scientific Report :
2007
Please use the identifier:
http://dx.doi.org/10.1063/1.2753835 in citations.
Please use the identifier: http://hdl.handle.net/2128/19080 in citations.
Folding of a Miniprotein with mixed Fold
Folding of a Miniprotein with mixed Fold
Using the 28 residue betabetaalpha protein FSD-EY as a target system, we examine correction terms for the ECEPP/3 force field. We find an increased probability of formation of the native state at low temperatures resulting from a reduced propensity to form alpha helices and increased formation of be...
Saved in:
Personal Name(s): | Mohanty, S. |
---|---|
Hansmann, U. H. E. | |
Contributing Institute: |
John von Neumann - Institut für Computing; NIC |
Published in: | The @journal of chemical physics, 127 (2007) S. 035102 |
Imprint: |
Melville, NY
American Institute of Physics
2007
|
Physical Description: |
035102 |
DOI: |
10.1063/1.2753835 |
PubMed ID: |
17655464 |
Document Type: |
Journal Article |
Research Program: |
Scientific Computing |
Series Title: |
Journal of Chemical Physics
127 |
Subject (ZB): | |
Link: |
Get full text OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/19080 in citations.
Using the 28 residue betabetaalpha protein FSD-EY as a target system, we examine correction terms for the ECEPP/3 force field. We find an increased probability of formation of the native state at low temperatures resulting from a reduced propensity to form alpha helices and increased formation of beta sheets. Our analysis of the observed folding events suggests that the C-terminal helix of FSD-EY is much more stable than the N-terminal beta hairpin and forms first. The hydrophobic groups of the helix provide a template which promotes the formation of the beta hairpin that is never observed to form without the helix. |