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A structural ensemble of hen egg-white lysozyme in aqueous solution based on 2043 NMR NOE, 3J-coupling and S2 order-parameter data

Abstract:
A set of 1630 NOE atom–atom distance upper bounds, 213 3J-coupling constant values and 200 S2 order-parameter values derived from experimental NMR data is used in molecular dynamics simulations of Hen Egg-White Lysozyme (HEWL) in aqueous solution in order to generate a Boltzmann-weighted structural ensemble for the protein in aqueous solution that is compatible with the 2043 NMR data. The two protein force fields used, the GROMOS 54A7 and 54A8 force fields, which only differ in the partial charges of the charged side chains and the chain termini of the protein, show comparable behavior. Analysis of the generated structural ensembles shows that the protein in aqueous solution adopts a greater variety of hydrogen-bond patterns than is suggested by the various X-ray crystal structures of the protein.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/acs.jpcb.5c06511

Authors

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Oxford college:
St Hilda's College
Role:
Author
ORCID:
0000-0001-5040-9267
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Role:
Author
ORCID:
0000-0002-9583-7019
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Role:
Author
ORCID:
0000-0003-4366-6120


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Funder identifier:
https://ror.org/018mejw64
Grant:
EXC 2075 - 390740016


Publisher:
American Chemical Society
Journal:
Journal of Physical Chemistry B More from this journal
Volume:
129
Issue:
51
Pages:
13174–13187
Publication date:
2025-12-12
Acceptance date:
2025-11-24
DOI:
EISSN:
1520-5207
ISSN:
1520-6106


Language:
English
Pubs id:
2351660
UUID:
uuid_cca0ce7c-8d76-4ef3-84f4-8cdb3ceb7109
Local pid:
pubs:2351660
Deposit date:
2025-12-18
ARK identifier:

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