Vibrational studies of the disulfide group in proteins. Part V. Correlation of SS stretch frequencies with the CCSS dihedral angle in known protein disulfide bridges
dc.contributor.author | Qian, Weili | en_US |
dc.contributor.author | Krimm, Samuel | en_US |
dc.date.accessioned | 2006-04-28T16:28:15Z | |
dc.date.available | 2006-04-28T16:28:15Z | |
dc.date.issued | 1992-04 | en_US |
dc.identifier.citation | Qian, Weili; Krimm, Samuel (1992)."Vibrational studies of the disulfide group in proteins. Part V. Correlation of SS stretch frequencies with the CCSS dihedral angle in known protein disulfide bridges." Biopolymers 32(4): 321-326. <http://hdl.handle.net/2027.42/37862> | en_US |
dc.identifier.issn | 0006-3525 | en_US |
dc.identifier.issn | 1097-0282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/37862 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1623126&dopt=citation | en_US |
dc.description.abstract | Normal mode calculations have been done on 92 disulfide bridges in 25 known protein structures in order to correlate the SS stretch frequency with the CCSS dihedral angle. It is possible to classify the frequencies into four major categories, which provide a more detailed classification scheme than previously proposed from dialkyl disulfide correlations. | en_US |
dc.format.extent | 426145 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 | Polymer and Materials Science | en_US |
dc.title | Vibrational studies of the disulfide group in proteins. Part V. Correlation of SS stretch frequencies with the CCSS dihedral angle in known protein disulfide bridges | 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 | Biophysics Research Division and Department of Physics, University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Biophysics Research Division and Department of Physics, University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.identifier.pmid | 1623126 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/37862/1/360320405_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/bip.360320405 | en_US |
dc.identifier.source | Biopolymers | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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