% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Hoffmann:207418,
author = {Hoffmann, Falk and Vancea, Ioan and Kamat, Sanjay G. and
Strodel, Birgit},
title = {{P}rotein {S}tructure {P}rediction: {A}ssembly of
{S}econdary {S}tructure {E}lements by {B}asin-{H}opping},
journal = {ChemPhysChem},
volume = {15},
number = {15},
issn = {1439-4235},
address = {Weinheim},
publisher = {Wiley-VCH Verl.},
reportid = {PUBDB-2015-01328},
pages = {3378 - 3390},
year = {2014},
note = {(c) WILEY-VCH Verlag GmbH $\&$ Co. KGaA},
abstract = {The prediction of protein tertiary structure from primary
structure remains a challenging task. One possible approach
to this problem is the application of basin-hopping global
optimization combined with an all-atom force field. In this
work, the efficiency of basin-hopping is improved by
introducing an approach that derives tertiary structures
from the secondary structure assignments of individual
residues. This approach is termed secondary-to-tertiary
basin-hopping and benchmarked for three miniproteins:
trpzip, trp-cage and ER-10. For each of the three
miniproteins, the secondary-to-tertiary basin-hopping
approach successfully and reliably predicts their
three-dimensional structure. When it is applied to larger
proteins, correctly folded structures are obtained. It can
be concluded that the assembly of secondary structure
elements using basin-hopping is a promising tool for de novo
protein structure prediction.},
cin = {EMBL},
ddc = {540},
cid = {I:(DE-H253)EMBL-20120731},
pnm = {No facility / HGF program None (POF2-890)},
pid = {G:(DE-H253)POF2-HGF-No-Prog-20130405},
experiment = {EXP:(DE-MLZ)NOSPEC-20140101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000343801200021},
pubmed = {pmid:25056272},
doi = {10.1002/cphc.201402247},
url = {https://bib-pubdb1.desy.de/record/207418},
}