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Enzyme kinetics / Protein families / Biomolecules / Protein domains / Allosteric regulation / G protein-coupled receptor / Cooperativity / Effector / Jean-Pierre Changeux / Biology / Chemistry / Proteins


Structure-based model of allostery predicts coupling between distant sites Patrick Weinkama,1, Jaume Ponsb, and Andrej Salia,1 a Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemist
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Document Date: 2014-08-23 13:21:27


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City

South San Francisco / La Jolla / /

Company

IBM / Hewlett-Packard / bRinat Laboratories / Ligand / Pfizer Inc. / Gilmore SA / NetApp / Intel / /

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Facility

California Institute / University of California / /

IndustryTerm

similar energy / chemical perturbation / large allosteric network / chemical frustration / energy landscape perspective / identified allosteric systems / given regulated site / reagents/analytic tools / large energy change / energy minima / energy landscapes / chemical species / allosteric network / distance energy / energy difference / energy functions / energy contributions / distant regulated site / potential energy functions / energy / energy function / minor chemical perturbation / energy landscape / average energy / important regulated site / allosteric networks / effector binding site / potential energy function / allosteric site / free energy excitations / cellular control systems / distant allosteric site / energy landscape theory / high-energy interactions / /

Organization

Assembly of Notch / Department of Pharmaceutical Chemistry / Department of Bioengineering and Therapeutic Sciences / Pharmaceutical Chemistry / and California Institute for Quantitative Biosciences / University of California at San Diego / University of California / San Francisco / /

Person

Riccardo Pellarin / Patrick Weinkama / Jaume Ponsb / Peter G. Wolynes / Andrej Salia / Ben Webb / /

Position

Author / /

ProvinceOrState

California / /

Technology

RAM / biosensors / DNA binding / spectroscopy / simulation / /

URL

www.pnas.org/lookup/suppl / www.pnas.org/cgi/doi/10.1073/pnas.1116274109 / /

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