http://purl.uniprot.org/citations/11327770 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11327770 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11327770 | http://www.w3.org/2000/01/rdf-schema#comment | "Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.2001.4570"xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.org/dc/terms/identifier | "doi:10.1006/jmbi.2001.4570"xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Yang J.C."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Yang J.C."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Walker J.E."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Walker J.E."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Videler H."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Videler H."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Runswick M.J."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Runswick M.J."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Carbajo R.J."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Carbajo R.J."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Neuhaus D."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Neuhaus D."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Gordon-Smith D.J."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/author | "Gordon-Smith D.J."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/pages | "325-339"xsd:string |
http://purl.uniprot.org/citations/11327770 | http://purl.uniprot.org/core/pages | "325-339"xsd:string |