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Journal article

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

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Publisher copy:
10.1021/acs.jpcb.7b03647

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Institution:
University of Oxford
Division:
MPLS
Department:
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
Source identifiers:
702492
Pubs id:
pubs:702492
UUID:
uuid:f7048ee9-967a-4852-8f6c-eb283dfb1e45
Local pid:
pubs:702492
Deposit date:
2017-06-30

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