Journal article
The fragment molecular orbital method reveals new insight into the chemical nature of GPCR-ligand interactions
- Abstract:
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Our interpretation of ligand–protein interactions is often informed by high-resolution structures, which represent the cornerstone of structure-based drug design. However, visual inspection and molecular mechanics approaches cannot explain the full complexity of molecular interactions. Quantum Mechanics approaches are often too computationally expensive, but one method, Fragment Molecular Orbital (FMO), offers an excellent compromise and has the potential to reveal key interactions that would...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
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(Preview, Accepted manuscript, pdf, 128.5KB, Terms of use)
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- Publisher copy:
- 10.1021/acs.jcim.5b00644
Authors
Funding
+ Biotechnology and Biological Sciences Research Council
More from this funder
Funding agency for:
Biggin, P
Grant:
BB/L026287/1
+ Engineering and Physical Sciences Research Council
More from this funder
Funding agency for:
Aldeghi, M
Bibliographic Details
- Publisher:
- American Chemical Society
- Journal:
- Journal of Chemical Information and Modeling More from this journal
- Volume:
- 56
- Issue:
- 1
- Pages:
- 159-172
- Publication date:
- 2015-12-07
- DOI:
- EISSN:
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1549-960X
- ISSN:
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1549-9596
Item Description
- Language:
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English
- Pubs id:
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pubs:587370
- UUID:
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uuid:e46e7d6d-0eda-4f95-8ab7-393e83d6f2f7
- Local pid:
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pubs:587370
- Source identifiers:
-
587370
- Deposit date:
-
2016-03-14
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2015
- Notes:
- © 2015 American Chemical Society. This is the accepted manuscript version of the article. The final version is available online from American Chemical Society at: 10.1021/acs.jcim.5b00644
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