Extended conformations of polypeptides and proteins in urea and guanidine hydrochloride
dc.contributor.author | Tiffany, M. Lois | en_US |
dc.contributor.author | Krimm, Samuel | en_US |
dc.date.accessioned | 2006-04-28T16:26:52Z | |
dc.date.available | 2006-04-28T16:26:52Z | |
dc.date.issued | 1973-03 | en_US |
dc.identifier.citation | Tiffany, M. Lois; Krimm, S. (1973)."Extended conformations of polypeptides and proteins in urea and guanidine hydrochloride." Biopolymers 12(3): 575-587. <http://hdl.handle.net/2027.42/37834> | en_US |
dc.identifier.issn | 0006-3525 | en_US |
dc.identifier.issn | 1097-0282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/37834 | |
dc.description.abstract | By analyzing the effect of urea and guanidine hydrochloride on the circular dichroism of many polypeptides and proteins, it is concluded that under conditions of high concentration of the perturbant and at low temperatures the resultant state approached is that of a local extended helix structure instead of a completely random coil. Intensification by urea and guanidine hydrochloride of the circular dichroism bands of poly- L -proline II leads to the proof that the mechanism of interaction of urea and guanidine hydrochloride with proteins is through hydrogen bonding to the backbone carbonyl group. | en_US |
dc.format.extent | 670685 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 | Extended conformations of polypeptides and proteins in urea and guanidine hydrochloride | 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 48104 | 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 48104 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/37834/1/360120310_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/bip.1973.360120310 | en_US |
dc.identifier.source | Biopolymers | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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