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Microcalorimetric studies of the heats of solution of bovine myelin basic protein

dc.contributor.authorRandall, Cynthia S.en_US
dc.contributor.authorZand, Roberten_US
dc.date.accessioned2006-04-07T18:56:50Z
dc.date.available2006-04-07T18:56:50Z
dc.date.issued1985-10-04en_US
dc.identifier.citationRandall, Cynthia S., Zand, Robert (1985/10/04)."Microcalorimetric studies of the heats of solution of bovine myelin basic protein." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 831(2): 242-248. <http://hdl.handle.net/2027.42/25538>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T21-47PNXGD-CW/2/923e0d159c5f444518830a7da8a91b84en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/25538
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2412590&dopt=citationen_US
dc.description.abstractHeats of solution for myelin basic protein have been determined using microcalorimetry. All aqueous systems studies yielded negative heats of solution; in contrast, trifluoroethanol produced a small positive heat of solution, while reaction with dimethyl sulfoxide was strikingly exothermic. The heat of interaction for native myelin basic protein with 8 M urea at pH 4.0, 29[deg]C, was found to be -79 +/- 16 kcal/mol. The significance of these results in terms of the protein's structural organization is discussed.en_US
dc.format.extent489587 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleMicrocalorimetric studies of the heats of solution of bovine myelin basic proteinen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumMacromolecular Research Center, Biophysics Research Division, Institute of Science and Technology, and Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationumMacromolecular Research Center, Biophysics Research Division, Institute of Science and Technology, and Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, U.S.A.en_US
dc.identifier.pmid2412590en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/25538/1/0000079.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0167-4838(85)90041-Xen_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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