Article

Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation- <i>π</i> contacts in proteins

2019-10-04

Abstract excerpt

Flexible protein regions containing cationic and aromatic side-chains exposed to solvent may form transient cation- π interactions with structural and functional roles. To evaluate their stability and identify important intramolecular cation- π contacts, a combination of free energy profiles estimated from umbrella sampling with molecular dynamics simulations and chemical shift perturbations (CSP) obtained from...

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Literature Corpus work: 0312b92f-e2a5-5c0a-8c86-0927fd806df5
DOI: 10.1101/793984

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