Vibrational analysis of peptides, polypeptides, and proteins. XXXII. Α-Poly( L -glutamic acid)
dc.contributor.author | Sengupta, Pradeep K. | en_US |
dc.contributor.author | Krimm, Samuel | en_US |
dc.date.accessioned | 2006-04-28T16:27:42Z | |
dc.date.available | 2006-04-28T16:27:42Z | |
dc.date.issued | 1985-08 | en_US |
dc.identifier.citation | Sengupta, Pradeep K.; Krimm, S. (1985)."Vibrational analysis of peptides, polypeptides, and proteins. XXXII. Α-Poly( L -glutamic acid)." Biopolymers 24(8): 1479-1491. <http://hdl.handle.net/2027.42/37851> | en_US |
dc.identifier.issn | 0006-3525 | en_US |
dc.identifier.issn | 1097-0282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/37851 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2412608&dopt=citation | en_US |
dc.description.abstract | The Raman and ir spectra of Α-helical poly( L -glutamic acid) have been assigned on the basis of a normal mode calculation for this structure. The force field was based on our previously refined main-chain force constants for Α-poly( L -alanine) and side-chain force constants for Β-calcium–poly( L -glutamate). Despite the identical backbone Α-helical structures, significantly different frequencies are calculated, and observed, in the amide III and backbone stretch regions of Α-poly( L -glutamic acid), as compared with Α-poly( L -alanine). This clearly demonstrates the influence of side-chain structure on mainchain vibrational modes. | en_US |
dc.format.extent | 689554 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 analysis of peptides, polypeptides, and proteins. XXXII. Α-Poly( L -glutamic acid) | 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, University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Biophysics Research Division, University of Michigan, Ann Arbor, Michigan 48109 | en_US |
dc.identifier.pmid | 2412608 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/37851/1/360240805_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/bip.360240805 | en_US |
dc.identifier.source | Biopolymers | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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