Zobrazeno 1 - 7
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pro vyhledávání: '"Kevin J. Woolley"'
Publikováno v:
Crystallization of Membrane Proteins ISBN: 9781351071277
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ac913b852d314486d14f716232a49ce
https://doi.org/10.1201/9781351071277-6
https://doi.org/10.1201/9781351071277-6
Autor:
Kevin J. Woolley
Publikováno v:
European Journal of Biochemistry. 166:127-130
Two c-type cytochromes were isolated from cells of the gram-negative bacterium Aquaspirillum itersonii grown under low aeration in the presence of nitrate. The major component, cytochrome c-550, was equated with the (single) c-type cytochrome previou
Autor:
Terry E. Meyer, Kevin J. Woolley
Publikováno v:
European Journal of Biochemistry. 163:161-166
A complete amino acid sequence for the rubredoxin from the photosynthetic bacterium Chlorobium thiosulphatophilum is proposed. The sequence, a single polypeptide chain of 53 amino acids, was deduced from the sequences of peptides obtained by chymotry
Autor:
Medha Athalye, Kevin J. Woolley
Publikováno v:
Biochemical and Biophysical Research Communications. 140:808-813
Principal Coordinate analysis (PCO) was applied to the comparison of protein sequences. A similarity matrix was derived from a dataset containing 21 c-type cytochrome sequences and this was analysed using PCO to produce a plot of the first three prin
Autor:
Kevin J. Woolley, Herbert Zuber, Jane Valentine, RenéA. Brunisholz, J. Gordon Lindsay, Richard J. Cogdell
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 849:295-303
The membrane location of the two B890-apoproteins from Rhodospirillum rubrum has been investigated by comparing the effects of mild proteolysis with proteinase K, and immunoprecipitation, with antibodies prepared against the B890-complex and its indi
Autor:
Kevin J. Woolley
Publikováno v:
European journal of biochemistry. 166(1)
A complete amino acid sequence is proposed for the cytochrome c-550 isolated from the gram-negative chemoorganotrophic bacterium Aquaspirillum itersonii. The sequence, a single polypeptide chain of 111 residues, was deduced from the sequences of pept
Publikováno v:
Biochemical Society Transactions. 14:57-57