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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

Authors


Ugolini, R More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Schwalbe, H More by this author
Journal:
Protein science : a publication of the Protein Society
Volume:
15
Issue:
6
Pages:
1397-1407
Publication date:
2006-06-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:087b2aed-2331-4b37-9d64-46a01c72271a
Source identifiers:
100798
Local pid:
pubs:100798

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