- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/pro.5560060620
-
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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
- Copyright date:
- 1997
Journal article
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
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