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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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Publisher copy:
10.1039/c7sc04905f

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
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Royal Society More from this funder
Science Without Borders More from this funder
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
Source identifiers:
832206
Keywords:
Pubs id:
pubs:832206
UUID:
uuid:7991a9ba-bcbd-4959-9dab-872a6f88368a
Local pid:
pubs:832206
Deposit date:
2018-04-04

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