- 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 ...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted Manuscript
- Files:
-
-
(pdf, 627.4KB)
-
(pdf, 942.8KB)
-
- Publisher copy:
- 10.1021/acs.jpcb.7b03647
-
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- 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
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2017
- Notes:
-
Copyright © 2017 American Chemical Society. This is the accepted manuscript version of the article. The final version is available online from American Chemical Society at: https://doi.org/10.1021/acs.jpcb.7b03647
Journal article
Using complementary NMR data sets to detect inconsistencies and model flaws in the structure determination of human interleukin-4
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