Selection originating from protein stability/foldability: relationships between protein folding free energy, sequence ensemble, and fitness

DOI10.1016/J.JTBI.2017.08.018zbMath1393.92041arXiv1612.09379OpenAlexW2747264980WikidataQ47899096 ScholiaQ47899096MaRDI QIDQ1748999

Sanzo Miyazawa

Publication date: 15 May 2018

Published in: Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL: https://arxiv.org/abs/1612.09379

zbMATH Keywords

Boltzmann distributionpositive selectionfolding free energy changeinverse statistical potentialselective temperature

Mathematics Subject Classification ID

Protein sequences, DNA sequences (92D20) Computational methods for problems pertaining to biology (92-08)

Related Items (1)

Cooperative ``folding transition in the sequence space facilitates function-driven evolution of protein families

Uses Software

• ProTherm
• Ace
• AWSEM-MD

Cites Work

• Selection maintaining protein stability at equilibrium
• Fast pseudolikelihood maximization for direct-coupling analysis of protein structure from many homologous amino-acid sequences
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