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.

By: J. Maciag n, S. Mackenzie n, M. Tucker n, J. Schipper n, P. Swartz n & A. Clark n

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
Source: Web Of Science
Added: August 6, 2018