Functional modulation of a protein folding landscape via side-chain distortion
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference39 articles.
1. The PDZ2 Domain of Syntenin at Ultra-high Resolution: Bridging the Gap Between Macromolecular and Small Molecule Crystallography
2. The 0.83Å Resolution Crystal Structure of α-Lytic Protease Reveals the Detailed Structure of the Active Site and Identifies a Source of Conformational Strain
3. Kinetics versus Thermodynamics in Protein Folding
4. Kinetic stability as a mechanism for protease longevity
5. Unfolded conformations of α-lytic protease are more stable than its native state
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1. Reframing prosegment‐dependent folding and limits on natural protein folding landscapes from an evolutionary perspective;Proteins: Structure, Function, and Bioinformatics;2023-04-04
2. Exploring the Evolutionary History of Kinetic Stability in the α-Lytic Protease Family;Biochemistry;2021-01-12
3. Exploring the evolutionary history of kinetic stability in the alpha-lytic protease family;2020-08-31
4. Kinetic trapping in protein folding;Protein Engineering, Design and Selection;2019-02
5. Planarity and out-of-plane vibrational modes of tryptophan and tyrosine in biomolecular modeling;Physical Chemistry Chemical Physics;2019
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