Side-chain rotamer changes upon ligand binding: common, crucial, correlate with entropy and rearrange hydrogen bonding | Zendy

Francis Gaudreault | Zendy; Matthieu Chartier | Zendy; Rafaël Najmanovich | Zendy

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Side-chain rotamer changes upon ligand binding: common, crucial, correlate with entropy and rearrange hydrogen bonding

Author(s) -

Francis Gaudreault,

Matthieu Chartier,

Rafaël Najmanovich

Publication year - 2012

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/bts395

Subject(s) - hydrogen bond , conformational isomerism , chemistry , conformational entropy , ligand (biochemistry) , entropy (arrow of time) , computational chemistry , thermodynamics , biochemistry , physics , molecule , organic chemistry , receptor

Protein movements form a continuum from large domain rearrangements (including folding and restructuring) to side-chain rotamer changes and small rearrangements. Understanding side-chain flexibility upon binding is important to understand molecular recognition events and predict ligand binding.

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