Learning about protein folding via potential functions
dc.contributor.author | Maiorov, Vladimir N. | en_US |
dc.contributor.author | Crippen, Gordon M. | en_US |
dc.date.accessioned | 2006-04-28T17:02:16Z | |
dc.date.available | 2006-04-28T17:02:16Z | |
dc.date.issued | 1994-10 | en_US |
dc.identifier.citation | Maiorov, V. N.; Crippen, G. M. (1994)."Learning about protein folding via potential functions." Proteins: Structure, Function, and Genetics 20(2): 167-173. <http://hdl.handle.net/2027.42/38520> | en_US |
dc.identifier.issn | 0887-3585 | en_US |
dc.identifier.issn | 1097-0134 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/38520 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7846026&dopt=citation | en_US |
dc.description.abstract | Over the last few years we have developed an empirical potential function that solves the protein structure recognition problem : given the sequence for an n -residue globular protein and a collection of plausible protein conformations, including the native conformation for that sequence, identify the correct, native conformation. Having determined this potential on the basis of only some 6500 native/nonnative pairs of structures for 58 proteins, we find it recognizes the native conformation for essentially all compact, soluble, globular proteins having known native conformations in comparisons with 10 4 to 10 6 reasonable alternative conformations apiece. In this sense, the potential encodes nearly all the essential features of globular protein conformational preference. In addition it “knows” about many additional factors in protein folding, such as the stabilization of multimeric proteins, quaternary structure, the role of disulfide bridges and ligands, pro proteins vs. processed proteins, and minimal strand lengths in globular proteins. Comparisons are made with other sorts of protein folding problems, and applications in protein conformational determination and prediction are discussed. © 1994 Wiley-Liss, Inc. | en_US |
dc.format.extent | 790801 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Biochemistry and Biotechnology | en_US |
dc.title | Learning about protein folding via potential functions | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | 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.affiliationum | College of Pharmacy, University of Michigan, Ann Arbor, Michigan 48109 ; College of Pharmacy, University of Michigan, Ann Arbor, MI 48109 | en_US |
dc.identifier.pmid | 7846026 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/38520/1/340200206_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/prot.340200206 | en_US |
dc.identifier.source | Proteins: Structure, Function, and Genetics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.