Journal article
Characterization of the unfolded state of bovine alpha-lactalbumin and comparison with unfolded states of homologous proteins.
- Abstract:
-
The unfolded states of three homologous proteins with a very similar fold have been investigated by heteronuclear NMR spectroscopy. Secondary structure propensities as derived from interpretation of chemical shifts and motional restrictions as evidenced by heteronuclear (15)N relaxation rates have been analyzed in the reduced unfolded states of hen lysozyme and the calcium-binding proteins bovine alpha-lactalbumin and human alpha-lactalbumin. For all three proteins, significant deviations fro...
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- Publication status:
- Published
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- Publisher copy:
- 10.1110/ps.051974506
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Authors
Bibliographic Details
- Journal:
- Protein science : a publication of the Protein Society
- Volume:
- 15
- Issue:
- 6
- Pages:
- 1397-1407
- Publication date:
- 2006-06-01
- DOI:
- EISSN:
-
1469-896X
- ISSN:
-
0961-8368
- Source identifiers:
-
100798
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:100798
- UUID:
-
uuid:087b2aed-2331-4b37-9d64-46a01c72271a
- Local pid:
- pubs:100798
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2006
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