Contact potential that recognizes the correct folding of globular proteins
dc.contributor.author | Maiorov, Vladimir N. | en_US |
dc.contributor.author | Grippen, Gordon M. | en_US |
dc.date.accessioned | 2006-04-10T15:02:33Z | |
dc.date.available | 2006-04-10T15:02:33Z | |
dc.date.issued | 1992-10-05 | en_US |
dc.identifier.citation | Maiorov, Vladimir N., Grippen, Gordon M. (1992/10/05)."Contact potential that recognizes the correct folding of globular proteins." Journal of Molecular Biology 227(3): 876-888. <http://hdl.handle.net/2027.42/29791> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WK7-4DMP463-8V/2/6096035f2d6254d288cf76a84a2a953a | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/29791 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1404392&dopt=citation | en_US |
dc.description.abstract | We have devised a continuous function of interresidue contacts in globular proteins such that the X-ray crystal structure has a lower function value than that of thousands of protein-like alternative conformations. Although we fit the adjustable parameters of the potential using only 10,000 alternative structures for a selected training set of 37 proteins, a grand total of 530,000 constraints was satisfied, derived from 73 proteins and their numerous alternative conformations. In every case where the native conformation is adequately globular and compact, according to objective criteria we have developed, the potential function always favors the native over all alternatives by a substantial margin. This is true even for an additional three proteins never used in any way in the fitting procedure. Conformations differing only slightly from the native, such as those coming from crystal structures of the same protein complexed with different ligands or from crystal structures of point mutants, have function values very similar to the native's and always less than those of alternatives derived from substantially different crystal structures. This holds for all 95 structures that are homologous to one or another of various proteins we used. Realizing that this potential should be useful for modeling the conformation of new protein sequences from the body of protein crystal structures, we suggest a test for deciding whether a nearly correct approximation to the native conformation has been found. | en_US |
dc.format.extent | 1559999 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Contact potential that recognizes the correct folding of globular proteins | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | 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, U.S.A. | en_US |
dc.contributor.affiliationum | College of Pharmacy, University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 1404392 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/29791/1/0000133.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0022-2836(92)90228-C | en_US |
dc.identifier.source | Journal of Molecular Biology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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