Works (1)
Updated: July 5th, 2023 15:38
2016 journal article
Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(41), E6080–E6088.
author keywords: allostery; conformational selection; saturation mutagenesis; protein solvation; protein structure
MeSH headings : Allosteric Regulation; Allosteric Site; Amino Acid Substitution; Caspase 3 / chemistry; Caspase 3 / genetics; Caspase 3 / metabolism; Catalytic Domain; Crystallography, X-Ray; Enzyme Activation; Models, Molecular; Molecular Conformation; Molecular Dynamics Simulation; Mutagenesis; Protein Binding; Protein Conformation; Protein Multimerization; Quantitative Structure-Activity Relationship; Solubility; Water / chemistry
open access via europepmc.org (repository)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
6. Clean Water and Sanitation
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
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