Analysis and modulation of protein stability.
Numerous site-directed mutagenesis experiments have provided new insights into the stabilizing role of the individual forces and interactions within a globular protein molecule. Some useful guidelines and procedures are now available for producing genetically more stable proteins. Examples are the introduction of disulfide bonds, ion-binding sites, salt bridges, hydrophobic residues or hydrogen bonds, and the improvement of hydrophobic packing or alpha-helix propensity. Moreover, it is now clearly recognized that thermophilic (and, in general, extremophilic) bacteria produce highly stable proteins and enzymes of practical interest.
Department of Organic Chemistry, University of Padua, Italy.
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D000595:Amino Acid Sequence; D004220:Disulfides / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D015202:Protein Engineering; D011506:Proteins / Q000737:chemistry*
D004220:Disulfides; D011506:Proteins