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Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.

Abstract:

The extent of deuterium labeling of hen lysozyme, its three-disulfide derivative, and the homologous alpha-lactalbumins, has been measured by both mass spectrometry and NMR. Different conformational states of the proteins were produced by varying the solution conditions. Alternate protein conformers were found to contain different numbers of 2H atoms. Furthermore, measurement in the gas phase of the mass spectrometer or directly in solution by NMR gave consistent results. The unique ability o...

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Publication status:
Published

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Publisher copy:
10.1002/pro.5560060620

Authors


Nettleton, EJ More by this author
Morgan, CJ More by this author
Miranker, A More by this author
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Journal:
Protein science : a publication of the Protein Society
Volume:
6
Issue:
6
Pages:
1316-1324
Publication date:
1997-06-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:40233b31-096b-436d-afe7-03900e93e322
Source identifiers:
59351
Local pid:
pubs:59351

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