Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference36 articles.
1. Modeling evolutionary landscapes: Mutational stability, topology, and superfunnels in sequence space
2. Understanding Protein Evolution: From Protein Physics to Darwinian Selection
3. Spin glasses and the statistical mechanics of protein folding.
4. Statistical mechanics of proteins with ‘‘evolutionary selected’’ sequences
5. Navigating the Folding Routes
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1. In vivo functional phenotypes from a computational epistatic model of evolution;Proceedings of the National Academy of Sciences;2024-01-29
2. Coevolutionary Information Captures Catalytic Functions and Reveals Divergent Roles of Terpene Synthase Interdomain Connections;Biochemistry;2024-01-11
3. Selection pressures on evolution of ribonuclease H explored with rigorous free–energy–based design;Proceedings of the National Academy of Sciences;2024-01-09
4. Sequence‐dependent and ‐independent information in a combined random energy model for protein folding and coding;Proteins: Structure, Function, and Bioinformatics;2023-12-29
5. Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors;Journal of Molecular Evolution;2023-11-13
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