TY  - JOUR
AU  - Irbäck, A.
AU  - Mitternacht, S.
AU  - Mohanty, S.
TI  - An effective all-­atom potential for proteins
JO  - PMC Biophysics
VL  - 2
SN  - 1757-5036
CY  - Berlin
PB  - Springer
M1  - PreJuSER-8935
SP  - 2
PY  - 2009
N1  - Record converted from VDB: 12.11.2012
AB  - We describe and test an implicit solvent all-atom potential for simulations of protein folding and aggregation. The potential is developed through studies of structural and thermodynamic properties of 17 peptides with diverse secondary structure. Results obtained using the final form of the potential are presented for all these peptides. The same model, with unchanged parameters, is furthermore applied to a heterodimeric coiled-coil system, a mixed alpha/beta protein and a three-helix-bundle protein, with very good results. The computational efficiency of the potential makes it possible to investigate the free-energy landscape of these 49-67-residue systems with high statistical accuracy, using only modest computational resources by today's standards.PACS Codes: 87.14.E-, 87.15.A-, 87.15.Cc.
LB  - PUB:(DE-HGF)16
C6  - pmid:19356242
C2  - pmc:PMC2696411
DO  - DOI:10.1186/1757-5036-2-2
UR  - https://juser.fz-juelich.de/record/8935
ER  -