TY  - JOUR
AU  - Mohanty, S.
AU  - Hansmann, U. H. E.
TI  - Folding of proteins with diverse folds
JO  - Biophysical journal
VL  - 91
SN  - 0006-3495
CY  - New York, NY
PB  - Rockefeller Univ. Press
M1  - PreJuSER-54183
SP  - 3537
PY  - 2006
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Computer Simulation
KW  - Models, Chemical
KW  - Models, Molecular
KW  - Models, Statistical
KW  - Protein Conformation
KW  - Protein Folding
KW  - Proteins: chemistry
KW  - Proteins: ultrastructure
KW  - Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:16950845
C2  - pmc:PMC1630465
UR  - <Go to ISI:>//WOS:000241702500003
DO  - DOI:10.1529/biophysj.106.087668
UR  - https://juser.fz-juelich.de/record/54183
ER  -