Conformation dependence of the SH and CS stretch frequencies of the cysteine residue
dc.contributor.author | Qian, Weili | en_US |
dc.contributor.author | Krimm, Samuel | en_US |
dc.date.accessioned | 2006-04-28T16:28:12Z | |
dc.date.available | 2006-04-28T16:28:12Z | |
dc.date.issued | 1992-11 | en_US |
dc.identifier.citation | Qian, Weili; Krimm, Samuel (1992)."Conformation dependence of the SH and CS stretch frequencies of the cysteine residue." Biopolymers 32(11): 1503-1518. <http://hdl.handle.net/2027.42/37861> | en_US |
dc.identifier.issn | 0006-3525 | en_US |
dc.identifier.issn | 1097-0282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/37861 | |
dc.description.abstract | In order to relate the observed SH and CS stretch frequencies of the cysteine residue in proteins more closely to its conformation, we have done normal mode calculations on a model for this structure, viz., (CCONH)(CNHCO)CHCH 2 SH. A range of ✗ 1 and ✗ 2 were studied, combined with the φ,Ψ of the Α-helix, Β-sheet, glutathione, and extended-helix conformations. The force field was a combination of a scaled ab initio force field of the -CH 2 SH group, obtained from ethanethiol and tested on 1-propanethiol and 3-thiol-N-methylpropionamide, and our empirical force field for the peptide group. The results provide more detailed structure–spectra correlations than are possible from experimental studies of model compounds. © 1992 John Wiley & Sons, Inc. | en_US |
dc.format.extent | 1131011 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 | Conformation dependence of the SH and CS stretch frequencies of the cysteine residue | 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.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/37861/1/360321109_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/bip.360321109 | en_US |
dc.identifier.source | Biopolymers | 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.