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(15)N NMR relaxation data reveal significant chemical exchange broadening in the alpha-domain of human alpha-lactalbumin.

Abstract:

Human alpha-lactalbumin (alpha-LA), a 123-residue calcium-binding protein, has been studied using (15)N NMR relaxation methods in order to characterize backbone dynamics of the native state at the level of individual residues. Relaxation data were collected at three magnetic field strengths and analyzed using the model-free formalism of Lipari and Szabo. The order parameters derived from this analysis are generally high, indicating a rigid backbone. A total of 46 residues required an exchange...

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Publication status:
Published

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Publisher copy:
10.1021/bi900023m

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Biochemistry
Volume:
48
Issue:
19
Pages:
4031-4039
Publication date:
2009-05-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:7396c9d0-3422-4438-95ec-aa9382d502fc
Source identifiers:
99771
Local pid:
pubs:99771

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