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Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP.

Abstract:

We have used tandem mass spectrometry to examine the stoichiometry and binding sites of trp molecules in various assemblies of the protein complex TRAP. The results show that TRAP forms oligomers containing 11 and 12 subunits. MS/MS experiments show that up to 11 trp molecules bind to the 12-mer but that during gas-phase dissociation 5 then 6 trp molecules are released reflecting the different gas-phase stabilities of the partially ligated forms. At high trp concentrations, the protein assemb...

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Publication status:
Published

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Publisher copy:
10.1021/ja0317170

Authors


McCammon, MG More by this author
Hernández, H More by this author
Robinson, CV More by this author
Journal:
Journal of the American Chemical Society
Volume:
126
Issue:
19
Pages:
5950-5951
Publication date:
2004-05-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:9796e612-a67d-4e56-93d2-04bd2751ca27
Source identifiers:
59259
Local pid:
pubs:59259

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