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231223s2010 xx |||||o 00| ||eng c |
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|a 10.1002/jcc.21365
|2 doi
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|a pubmed24n0632.xml
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|a eng
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|a Maupetit, Julien
|e verfasserin
|4 aut
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|a A fast method for large-scale de novo peptide and miniprotein structure prediction
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|c 2010
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 16.04.2010
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|a Date Revised 03.02.2010
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|a published: Print
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|a Citation Status MEDLINE
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|a (c) 2009 Wiley Periodicals, Inc.
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|a Although peptides have many biological and biomedical implications, an accurate method predicting their equilibrium structural ensembles from amino acid sequences and suitable for large-scale experiments is still missing. We introduce a new approach-PEP-FOLD-to the de novo prediction of peptides and miniproteins. It first predicts, in the terms of a Hidden Markov Model-derived structural alphabet, a limited number of local conformations at each position of the structure. It then performs their assembly using a greedy procedure driven by a coarse-grained energy score. On a benchmark of 52 peptides with 9-23 amino acids, PEP-FOLD generates lowest-energy conformations within 2.8 and 2.3 A Calpha root-mean-square deviation from the full nuclear magnetic resonance structures (NMR) and the NMR rigid cores, respectively, outperforming previous approaches. For 13 miniproteins with 27-49 amino acids, PEP-FOLD reaches an accuracy of 3.6 and 4.6 A Calpha root-mean-square deviation for the most-native and lowest-energy conformations, using the nonflexible regions identified by NMR. PEP-FOLD simulations are fast-a few minutes only-opening therefore, the door to in silico large-scale rational design of new bioactive peptides and miniproteins
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|a Journal Article
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|a Peptides
|2 NLM
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| 650 |
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|a Proteins
|2 NLM
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|a Derreumaux, Philippe
|e verfasserin
|4 aut
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| 700 |
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|a Tufféry, Pierre
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of computational chemistry
|d 1984
|g 31(2010), 4 vom: 01. März, Seite 726-38
|w (DE-627)NLM098138448
|x 1096-987X
|7 nnns
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| 773 |
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|g volume:31
|g year:2010
|g number:4
|g day:01
|g month:03
|g pages:726-38
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| 856 |
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|u http://dx.doi.org/10.1002/jcc.21365
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