Escapement mechanisms: Efficient free energy transduction by reciprocally‐coupled gating

Conversion of the free energy of NTP hydrolysis efficiently into mechanical work and/or information by transducing enzymes sustains living systems far from equilibrium, and so has been of interest for many decades. Detailed molecular mechanisms, however, remain puzzling and incomplete. We previously...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2020-05, Vol.88 (5), p.710-717
1. Verfasser:	Carter, Charles W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism allosteric control Allosteric Regulation Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Biocatalysis Biomechanical Phenomena Catalysis Catalytic Domain Cations, Divalent combinatorial mutagenesis Computer applications Coupling (molecular) Domains energetic coupling Energy transduction far from equilibrium Free energy free energy surfaces Gating Geobacillus stearothermophilus - chemistry Geobacillus stearothermophilus - enzymology Geobacillus stearothermophilus - genetics Hydrolysis Kinetics Magnesium Magnesium - chemistry Magnesium - metabolism Models, Molecular Molecular modelling NTP hydrolysis Pendulums Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Signal Transduction Substrate Specificity Thermodynamics transducing enzymes tRNA Trp Tryptophan Tryptophan - chemistry Tryptophan - metabolism Tryptophan-tRNA Ligase - chemistry Tryptophan-tRNA Ligase - genetics Tryptophan-tRNA Ligase - metabolism
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