This title appears in the Scientific Report :
2007
Please use the identifier:
http://dx.doi.org/10.1103/PhysRevE.76.012901 in citations.
Please use the identifier: http://hdl.handle.net/2128/9229 in citations.
Improving an all-atom force field
Improving an all-atom force field
Experimentally well-characterized proteins that are small enough to be computationally tractable provide useful information for refining existing all-atom force fields. This is used by us for reparametrizing a recently developed all-atom force field. Relying on high statistics parallel tempering sim...
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Personal Name(s): | Mohanty, S. |
---|---|
Hansmann, U. H. E. | |
Contributing Institute: |
John von Neumann - Institut für Computing; NIC |
Published in: | Physical Review E Physical review / E, 76 76 (2007 2007) 1 1, S. 012901 012901 |
Imprint: |
College Park, Md.
APS
2007
2007-07-18 2007-07-01 |
Physical Description: |
012901 |
DOI: |
10.1103/PhysRevE.76.012901 |
Document Type: |
Journal Article |
Research Program: |
Scientific Computing |
Series Title: |
Physical Review E
76 |
Subject (ZB): | |
Link: |
Get full text OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/9229 in citations.
Experimentally well-characterized proteins that are small enough to be computationally tractable provide useful information for refining existing all-atom force fields. This is used by us for reparametrizing a recently developed all-atom force field. Relying on high statistics parallel tempering simulations of a designed 20 residue beta-sheet peptide, we propose incremental changes that improve the force field's range of applicability. |