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.
Fontana
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Department of Organic Chemistry, University of Padua, Italy.
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