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@ARTICLE{Mohanty:133447,
author = {Mohanty, Sandipan and Meinke, Jan and Zimmermann, Olav},
title = {{F}olding of {T}op7 in unbiased all-atom {M}onte {C}arlo
simulations},
journal = {Proteins},
volume = {81},
number = {8},
issn = {0887-3585},
address = {New York, NY},
publisher = {Wiley-Liss},
reportid = {FZJ-2013-01895},
pages = {1446 - 1456},
year = {2013},
abstract = {For computational studies of protein folding, proteins with
both helical and β-sheet secondary structure elements are
very challenging, since they expose subtle biases of the
physical models. Here we present reproducible folding of a
92 residue α/β protein (residues 3–94 of Top7, PDB ID:
1QYS) in computer simulations starting from random initial
conformations using a transferable physical model which has
been previously shown to describe the folding and
thermodynamic properties of about 20 other smaller proteins
of different folds. Top7 is a de novo designed protein with
two α-helices and a 5 stranded β-sheet. Experimentally it
is known to be unusually stable for its size, and its
folding transition distinctly deviates from the two state
behaviour commonly seen in natural single domain proteins.
In our all-atom implicit solvent parallel tempering Monte
Carlo simulations, Top7 shows a rapid transition to a group
of states with high native-like secondary structure, and a
much slower subsequent transition to the native state with a
root mean square deviation of about 3.5 Å from the
experimentally determined structure. Consistent with
experiments, we find Top7 to be thermally extremely stable,
although the simulations also find a large number of very
stable non-native states with high native-like secondary
structure.},
cin = {JSC},
ddc = {540},
cid = {I:(DE-Juel1)JSC-20090406},
pnm = {411 - Computational Science and Mathematical Methods
(POF2-411)},
pid = {G:(DE-HGF)POF2-411},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000329220400014},
pubmed = {pmid:23553942},
doi = {10.1002/prot.24295},
url = {https://juser.fz-juelich.de/record/133447},
}