Circular dichroism of the “random” polypeptide chain
dc.contributor.author | Tiffany, M. Lois | en_US |
dc.contributor.author | Krimm, Samuel | en_US |
dc.date.accessioned | 2006-04-28T16:26:25Z | |
dc.date.available | 2006-04-28T16:26:25Z | |
dc.date.issued | 1969-09 | en_US |
dc.identifier.citation | Tiffany, M. Lois; Krimm, S. (1969)."Circular dichroism of the “random” polypeptide chain." Biopolymers 8(3): 347-359. <http://hdl.handle.net/2027.42/37825> | en_US |
dc.identifier.issn | 0006-3525 | en_US |
dc.identifier.issn | 1097-0282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/37825 | |
dc.description.abstract | The circular dichroism (CD) spectrum of an unordered polypeptide chain does not correspond, as has been assumed heretofore, to that of a charged chain such as poly- L -glutamic acid or poly- L -lysine. The latter have been shown to have locally ordered structures with characteristic CD spectra. We have now obtained CD spectra of the unordered forms of the above synthetic, polypeptides, as well as of two fibrous proteins (collagen and feather keratin) and a globular protein (myoglobin). These spectra are all similar to that of unordered polyproline, having a negative band in the vicinity of 2000 mΜ and no additional bands at longer wavelengths. The lack of structural uniqueness of the unordered polypeptide chain is emphasized by these studies. | en_US |
dc.format.extent | 693731 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 | Circular dichroism of the “random” polypeptide chain | 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, Institute of Science and Technology and Harrison M. Randall Laboratory of Physics, University of Michigan, Ann Arbor, Michigan 48107 | en_US |
dc.contributor.affiliationum | Biophysics Research Division, Institute of Science and Technology and Harrison M. Randall Laboratory of Physics, University of Michigan, Ann Arbor, Michigan 48107 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/37825/1/360080306_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/bip.1969.360080306 | en_US |
dc.identifier.source | Biopolymers | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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