Allosteric switch regulates protein-protein binding through collective motion

Proceedings of the National Academy of Sciences of the United States of America

Volumn 113, Issue 12, 2016, Pages 3269-3274

  Smith, Colin A ^a   Ban, David ^a,b   Pratihar, Supriya ^a   Giller, Karin ^a   Paulat, Maria ^a   Becker, Stefan ^a   Griesinger, Christian ^a   Lee, Donghan ^a,b   De Groot, Bert L ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b University of Louisville School of Medicine   (United States)

Author keywords

Allostery; Concerted motion; Nuclear magnetic resonance; Protein dynamics; Relaxation dispersion

Indexed keywords

ALLOSTERISM; ARTICLE; BINDING AFFINITY; COLLECTIVE MOTION; CRYSTAL STRUCTURE; DISPERSION; MOLECULAR DYNAMICS; MOTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; REGULATORY MECHANISM; TEMPERATURE DEPENDENCE; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS;

PROTEIN; PROTEIN BINDING;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEINS;

EID: 84962217637     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1519609113     Document Type: Article

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