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Extended conformations of polypeptides and proteins in urea and guanidine hydrochloride

dc.contributor.authorTiffany, M. Loisen_US
dc.contributor.authorKrimm, Samuelen_US
dc.date.accessioned2006-04-28T16:26:52Z
dc.date.available2006-04-28T16:26:52Z
dc.date.issued1973-03en_US
dc.identifier.citationTiffany, 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.issn0006-3525en_US
dc.identifier.issn1097-0282en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/37834
dc.description.abstractBy 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.extent670685 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherChemistryen_US
dc.subject.otherPolymer and Materials Scienceen_US
dc.titleExtended conformations of polypeptides and proteins in urea and guanidine hydrochlorideen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology, and Harrison M. Randall Laboratory of Physics, University of Michigan, Ann Arbor, Michigan 48104en_US
dc.contributor.affiliationumBiophysics Research Division, Institute of Science and Technology, and Harrison M. Randall Laboratory of Physics, University of Michigan, Ann Arbor, Michigan 48104en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/37834/1/360120310_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/bip.1973.360120310en_US
dc.identifier.sourceBiopolymersen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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