Positive and negative design in stability and thermal adaptation of natural proteins

• Main Authors: Berezovsky I.N., Zeldovich K.B., Shakhnovich E.I.
• Other Authors: BIOLOGICAL SCIENCES
• Format: Article
• Published: 2019
• Subjects: proteome; archaeal protein; amino acid composition; amino acid sequence; article; environmental factor; hydrophobicity; molecular model; mutation; protein analysis; protein conformation; protein folding; protein interaction; protein stability; protein structure; temperature dependence; chemical model; chemical phenomena; chemical structure; chemistry; computer simulation; drug stability; methodology; molecular genetics; protein denaturation; sequence alignment; sequence analysis; structure activity relation; temperature; ultrastructure; Amino Acid Sequence; Archaeal Proteins; Computer Simulation; Drug Stability; Hydrophobic and Hydrophilic Interactions; Models, Chemical; Models, Molecular; Molecular Sequence Data; Protein Denaturation; Protein Folding; Sequence Alignment; Sequence Analysis, Protein; Structure-Activity Relationship; Temperature
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/161869
• Institution: National University of Singapore

10.1371/journal.pcbi.0030052