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Is human thioredoxin monomeric or dimeric?
Author(s) -
Gronenborn Angela M.,
Clore G. Marius,
Louis John M.,
Wingfield Paul T.
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.2.426
Subject(s) - thioredoxin , nuclear magnetic resonance spectroscopy , chemistry , monomer , methionine , amino acid , biochemistry , ferredoxin thioredoxin reductase , stereochemistry , thioredoxin reductase , enzyme , organic chemistry , polymer
We have examined the molecular weight and rotational correlation time of human thioredoxin by analytical ultracentrifugation and NMR spectroscopy, respectively. Two variants of human thioredoxin were studied, namely human thioredoxin identical in amino acid sequence to the one whose NMR structure we previously determined (C62A, C69A, C73A, M74T) and human thioredoxin (C62A, C69A, C73A, M74) containing the wild‐type amino acid methionine at position 74. In both cases, the experimental data indicate that the predominant species is monomeric and we find no evidence for the existence of a well‐defined dimeric form as was observed in the recently reported crystal structure (Weichsel et al., 1996) of human thioredoxin and the C73S mutant.