dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUNAERP
dc.date.accessioned2014-05-20T13:49:23Z
dc.date.accessioned2022-10-05T14:20:51Z
dc.date.available2014-05-20T13:49:23Z
dc.date.available2022-10-05T14:20:51Z
dc.date.created2014-05-20T13:49:23Z
dc.date.issued2005-11-01
dc.identifierProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 12, n. 8, p. 819-822, 2005.
dc.identifier0929-8665
dc.identifierhttp://hdl.handle.net/11449/17599
dc.identifier10.2174/0929866054864283
dc.identifierWOS:000232811400017
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3892263
dc.description.abstractBnSP-7 and BnSP-6, two Lys49-phospholipase A(2) isolated from Bothrops neuwiedi pauloensis snake venom, were co-crystallized with a-tocopherol and X-ray diffraction data were collected for both complexes (2.2 and 2.6 angstrom). A new alternative quaternary conformation for these two complexes compared with all other dimeric Lys49-PLA(2) has been observed.
dc.languageeng
dc.publisherBentham Science Publ Ltd
dc.relationProtein and Peptide Letters
dc.relation1.039
dc.relation0,429
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectcrystallization
dc.subjectX-ray crystallography
dc.subjectLys49-phospholipase A(2)
dc.subjectBothrops neuwiedi venom
dc.subjectmyotoxity
dc.subjectalpha-tocopherol
dc.titleCrystallization and preliminary X-ray diffraction studies of two myotoxic Lys49-phospholipases A(2) complexed with alpha-tocopherol
dc.typeArtigo


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