Journal article
Cation-π interactions in protein-ligand binding: Theory and data-mining reveal different roles for lysine and arginine
- Abstract:
-
We have studied the cation–p interactions of neutral aromatic ligands with the cationic amino acid residues arginine, histidine and lysine using ab initio calculations, symmetry adapted perturbation theory (SAPT), and a systematic meta-analysis of all available Protein Data Bank (PDB) X-ray structures. Quantum chemical potential energy surfaces (PES) for these interactions were obtained at the DLPNO-CCSD(T) level of theory and compared against the empirical distribution of 2012 unique protein...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Funding
Science Without Borders
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World Bank
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Royal Society
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Bibliographic Details
- Publisher:
- Royal Society of Chemistry Publisher's website
- Journal:
- Chemical Science Journal website
- Volume:
- 9
- Issue:
- 10
- Pages:
- 2655-2665
- Publication date:
- 2018-01-31
- Acceptance date:
- 2018-01-20
- DOI:
- EISSN:
-
2041-6539
- ISSN:
-
2041-6520
Item Description
- Keywords:
- Pubs id:
-
pubs:832206
- UUID:
-
uuid:7991a9ba-bcbd-4959-9dab-872a6f88368a
- Local pid:
- pubs:832206
- Source identifiers:
-
832206
- Deposit date:
- 2018-04-04
Terms of use
- Copyright holder:
- Royal Society of Chemistry
- Copyright date:
- 2018
- Notes:
- © The Royal Society of Chemistry 2018. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence.
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