Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs.
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The ensemble nature of allosteryThe Designability of Protein Switches by Chemical Rescue of Structure: Mechanisms of Inactivation and ReactivationEngineering of temperature- and light-switchable Cas9 variantsRational design of a fusion protein to exhibit disulfide-mediated logic gate behavior.Modular protein switches derived from antibody mimetic proteins.Development of a cancer-marker activated enzymatic switch from the herpes simplex virus thymidine kinase.Design of protein switches based on an ensemble model of allosteryThe interplay between effector binding and allostery in an engineered protein switch.Enzymatic protein switches built from paralogous input domains.Creation of Antigen-Dependent β-Lactamase Fusion Protein Tethered by Circularly Permuted Antibody Variable Domains.
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P2860
Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs.
description
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name
Non-allosteric enzyme switches ...... than their non-switch analogs.
@en
Non-allosteric enzyme switches ...... than their non-switch analogs.
@nl
type
label
Non-allosteric enzyme switches ...... than their non-switch analogs.
@en
Non-allosteric enzyme switches ...... than their non-switch analogs.
@nl
prefLabel
Non-allosteric enzyme switches ...... than their non-switch analogs.
@en
Non-allosteric enzyme switches ...... than their non-switch analogs.
@nl
P2093
P2860
P356
P1433
P1476
Non-allosteric enzyme switches ...... than their non-switch analogs.
@en
P2093
Angela San
Jay H Choi
Marc Ostermeier
P2860
P304
P356
10.1002/PRO.2234
P577
2013-03-08T00:00:00Z