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| Home > Publications database > Understanding protein folding: Small proteins in silico > print |
| 001 | 62830 | ||
| 005 | 20180211164010.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:18036571 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC2244683 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.bbapap.2007.10.010 |
| 024 | 7 | _ | |2 WOS |a WOS:000253013200025 |
| 037 | _ | _ | |a PreJuSER-62830 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |a Zimmermann, O. |b 0 |u FZJ |0 P:(DE-Juel1)132307 |
| 245 | _ | _ | |a Understanding protein folding: Small proteins in silico |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2008 |
| 300 | _ | _ | |a 252 - 258 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |a BBA - Proteins and Proteomics |x 1570-9639 |0 19421 |y 1 |v 1784 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Recent improvements in methodology and increased computer power now allow atomistic computer simulations of protein folding. We briefly review several advanced Monte Carlo algorithms that have contributed to this development. Details of folding simulations of three designed mini proteins are shown. Adding global translations and rotations has allowed us to handle multiple chains and to simulate the aggregation of six beta-amyloid fragments. In a different line of research we have developed several algorithms to predict local features from sequence. In an outlook we sketch how such biasing could extend the application spectrum of Monte Carlo simulations to structure prediction of larger proteins. |
| 536 | _ | _ | |a Scientific Computing |c P41 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK411 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Algorithms |
| 650 | _ | 2 | |2 MeSH |a Computational Biology: methods |
| 650 | _ | 2 | |2 MeSH |a Computer Simulation |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Monte Carlo Method |
| 650 | _ | 2 | |2 MeSH |a Protein Conformation |
| 650 | _ | 2 | |2 MeSH |a Protein Folding |
| 650 | _ | 2 | |2 MeSH |a Proteins: chemistry |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Proteins |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a protein folding |
| 653 | 2 | 0 | |2 Author |a aggregation |
| 653 | 2 | 0 | |2 Author |a generalized-ensemble sampling |
| 653 | 2 | 0 | |2 Author |a structure prediction |
| 700 | 1 | _ | |a Hansmann, U. H. E. |b 1 |u FZJ |0 P:(DE-Juel1)VDB46160 |
| 773 | _ | _ | |a 10.1016/j.bbapap.2007.10.010 |g Vol. 1784, p. 252 - 258 |p 252 - 258 |q 1784<252 - 258 |0 PERI:(DE-600)2209540-8 |t Biochimica et biophysica acta / Proteins and proteomics |v 1784 |y 2008 |x 1570-9639 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2244683 |
| 909 | C | O | |o oai:juser.fz-juelich.de:62830 |p VDB |
| 913 | 1 | _ | |k P41 |v Scientific Computing |l Supercomputing |b Schlüsseltechnologien |0 G:(DE-Juel1)FUEK411 |x 0 |
| 914 | 1 | _ | |y 2008 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k NIC |l John von Neumann - Institut für Computing |g NIC |0 I:(DE-Juel1)NIC-20090406 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)99681 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)NIC-20090406 |
| 980 | _ | _ | |a UNRESTRICTED |
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