Toward Correct Protein Folding Potentials
dc.contributor.author | Chhajer, Mukesh | en_US |
dc.contributor.author | Crippen, Gordon M. | en_US |
dc.date.accessioned | 2006-09-08T21:01:08Z | |
dc.date.available | 2006-09-08T21:01:08Z | |
dc.date.issued | 2004-06 | en_US |
dc.identifier.citation | Chhajer, M.; Crippen, G.M.; (2004). "Toward Correct Protein Folding Potentials." Journal of Biological Physics 30(2): 171-185. <http://hdl.handle.net/2027.42/43055> | en_US |
dc.identifier.issn | 0092-0606 | en_US |
dc.identifier.issn | 1573-0689 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/43055 | |
dc.description.abstract | Empirical protein folding potentialfunctions should have a global minimum nearthe native conformationof globular proteins that fold stably, andthey should give the correct free energy offolding. We demonstrate that otherwise verysuccessful potentials fail to have even alocal minimumanywhere near the native conformation, anda seemingly well validated method ofestimatingthe thermodynamic stability of the nativestate is extremely sensitive to smallperturbations inatomic coordinates. These are bothindicative of fitting a great deal ofirrelevant detail. Here weshow how to devise a robust potentialfunction that succeeds very well at bothtasks, at least for alimited set of proteins, and this involvesdeveloping a novel representation of thedenatured state.Predicted free energies of unfolding for 25mutants of barnase are in close agreementwith theexperimental values, while for 17 mutantsthere are substantial discrepancies. | en_US |
dc.format.extent | 135105 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; Springer Science+Business Media | en_US |
dc.subject.other | Physics | en_US |
dc.subject.other | Polymer Sciences | en_US |
dc.subject.other | Statistical Physics | en_US |
dc.subject.other | Condensed Matter | en_US |
dc.subject.other | Biophysics/Biomedical Physics | en_US |
dc.subject.other | Barnase | en_US |
dc.subject.other | Decoys | en_US |
dc.subject.other | Denatured State | en_US |
dc.subject.other | Protein Folding | en_US |
dc.subject.other | Thermodynamic Stability | en_US |
dc.title | Toward Correct Protein Folding Potentials | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Physics | en_US |
dc.subject.hlbsecondlevel | Mathematics | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | College of Pharmacy, University of Michigan, Ann Arbor, MI, 48109-1065, U.S.A | en_US |
dc.contributor.affiliationother | Department of Chemistry, University of North Carolina, Chapel Hill, NC, 27599, U.S.A | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 23345867 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/43055/1/10867_2004_Article_5139201.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/B:JOBP.0000035854.68334.dd | en_US |
dc.identifier.source | Journal of Biological Physics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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