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Using complementary NMR data sets to detect inconsistencies and model flaws in the structure determination of human interleukin-4

Abstract:

The derivation of protein structure from values of observable quantities measured in NMR experiments is a rather non-trivial task due to (i) the limited number of data compared to degrees of freedom of a protein, (ii) the uncertainty inherent to the function connecting an observable quantity to molecular structure, (iii) the finite quality of biomolecular models and force fields used in structure refinement, and (iv) the conformational freedom of a protein in aqueous solution, which requires ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

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Publisher copy:
10.1021/acs.jpcb.7b03647

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Department:
Oxford, MPLS, Chemistry
Role:
Author
Publisher:
American Chemical Society Publisher's website
Journal:
Journal of Physical Chemistry Journal website
Volume:
121
Issue:
29
Pages:
7055–7063
Publication date:
2017-06-22
Acceptance date:
2017-06-22
DOI:
ISSN:
0022-3654
Pubs id:
pubs:702492
URN:
uri:f7048ee9-967a-4852-8f6c-eb283dfb1e45
UUID:
uuid:f7048ee9-967a-4852-8f6c-eb283dfb1e45
Local pid:
pubs:702492
Paper number:
29

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