ProTherm

swMATH16247MaRDI QIDQ28117FDOQ28117

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Cited In (5)

• Global stability of protein folding from an empirical free energy function
• Physics and chemistry-driven artificial neural network for predicting bioactivity of peptides and proteins and their design
• Selection maintaining protein stability at equilibrium
• Selection originating from protein stability/foldability: relationships between protein folding free energy, sequence ensemble, and fitness
• Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymes

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