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Amino acid sequence of the flavodoxin
dc.contributor.authorTanaka, Masaruen_US
dc.contributor.authorHaniu, Mitsuruen_US
dc.contributor.authorYasunobu, Kerry T.en_US
dc.contributor.authorMayhew, Stephen G.en_US
dc.contributor.authorMassey, Vincenten_US
dc.date.accessioned2006-04-17T16:23:21Z
dc.date.available2006-04-17T16:23:21Z
dc.date.issued1971-08-20en_US
dc.identifier.citationTanaka, Masaru, Haniu, Mitsuru, Yasunobu, Kerry T., Mayhew, Stephen, Massey, Vincent (1971/08/20)."Amino acid sequence of the flavodoxin." Biochemical and Biophysical Research Communications 44(4): 886-892. <http://hdl.handle.net/2027.42/33577>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DPC7R4-T0/2/838b31d77662b589f02705e78ce65bf1en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/33577
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5125231&dopt=citationen_US
dc.description.abstractThe amino acid sequence of the flavodoxin has been determined except for a few residues. The protein contains 137 amino acid residues and the NH2- and COOH-terminal residues are methionine and alanine respectively. The protein contains two cysteine residues in positions 54 and 127. However, the cysteine residue in position 127 appears to be involved in binding FMN and therefore the active site is located near the COOH-terminal position of the protein. There are no aromatic amino acid residues in this region of the protein.en_US
dc.format.extent366325 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleAmino acid sequence of the flavodoxinen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry-Biophysics, University of Hawaii, Honolulu, Hawaii, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry-Biophysics, University of Hawaii, Honolulu, Hawaii, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry-Biophysics, University of Hawaii, Honolulu, Hawaii, USAen_US
dc.identifier.pmid5125231en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/33577/1/0000080.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(71)90794-7en_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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