Determination of an empirical energy function for protein conformational analysis by energy embedding
dc.contributor.author | Crippen, Gordon M. | en_US |
dc.contributor.author | Ponnuswamy, P. K. | en_US |
dc.date.accessioned | 2006-04-28T16:49:46Z | |
dc.date.available | 2006-04-28T16:49:46Z | |
dc.date.issued | 1987-10 | en_US |
dc.identifier.citation | Crippen, Gordon M.; Ponnuswamy, P. K. (1987)."Determination of an empirical energy function for protein conformational analysis by energy embedding." Journal of Computational Chemistry 8(7): 972-981. <http://hdl.handle.net/2027.42/38277> | en_US |
dc.identifier.issn | 0192-8651 | en_US |
dc.identifier.issn | 1096-987X | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/38277 | |
dc.description.abstract | It is quite easy to propose an empirical potential for conformational analysis such that given crystal structures lie near local minima. What is much more difficult, is to devise a function such that the native structure lies near a relatively deep local minimum, at least in some neighborhood of the native in conformation space. An algorithm is presented for finding such a potential acting on proteins where each amino acid residue is represented by a single point. When the given structure is either an Α-helical, Β-strand, or hairpin bend segment of pancreatic trypsin inhibitor, the resulting potential function in each case possesses a deep minimum within 0.10 Å of the native conformation. The improved energy embedding algorithm locates a marginally better minimum in each case only 0.1–1.3 Å away from the respective native state. In other words, this potential function guides a conformational search toward structures very close to the native over a wide range of conformation space. | en_US |
dc.format.extent | 982291 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | John Wiley & Sons, Inc. | en_US |
dc.subject.other | Computational Chemistry and Molecular Modeling | en_US |
dc.subject.other | Biochemistry | en_US |
dc.title | Determination of an empirical energy function for protein conformational analysis by energy embedding | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbtoplevel | Engineering | 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, Michigan 48109 | en_US |
dc.contributor.affiliationother | Department of Physics, Bharathidasan University, Tiruchirapalli-620 023, Tamilnadu, India | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/38277/1/540080707_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/jcc.540080707 | en_US |
dc.identifier.source | Journal of Computational Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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