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@ARTICLE{Mohanty:54183,
author = {Mohanty, S. and Hansmann, U. H. E.},
title = {{F}olding of proteins with diverse folds},
journal = {Biophysical journal},
volume = {91},
issn = {0006-3495},
address = {New York, NY},
publisher = {Rockefeller Univ. Press},
reportid = {PreJuSER-54183},
pages = {3537},
year = {2006},
note = {Record converted from VDB: 12.11.2012},
abstract = {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.},
keywords = {Computer Simulation / Models, Chemical / Models, Molecular
/ Models, Statistical / Protein Conformation / Protein
Folding / Proteins: chemistry / Proteins: ultrastructure /
Proteins (NLM Chemicals) / J (WoSType)},
cin = {NIC},
ddc = {570},
cid = {I:(DE-Juel1)NIC-20090406},
pnm = {Scientific Computing},
pid = {G:(DE-Juel1)FUEK411},
shelfmark = {Biophysics},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:16950845},
pmc = {pmc:PMC1630465},
UT = {WOS:000241702500003},
doi = {10.1529/biophysj.106.087668},
url = {https://juser.fz-juelich.de/record/54183},
}