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Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin.

Abstract:

The quaternary structure of the polydisperse mammalian chaperone alphaB-crystallin, a member of the small heat-shock protein family, has been investigated by using electrospray mass spectrometry. The intact assemblies give rise to mass spectra that are complicated by the overlapping of charge states from the different constituent oligomers. Therefore, to determine which oligomers are formed by this protein, tandem mass spectrometry experiments were performed. The spectra reveal a distribution...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.1932958100

Authors


Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
100
Issue:
19
Pages:
10611-10616
Publication date:
2003-09-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:c52ca492-3aa3-4527-8666-66a584656b2c
Source identifiers:
59251
Local pid:
pubs:59251

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