Finding the fittest fold: using the evolutionary record to design new proteins.
For many years, the holy grail of protein engineering has been the design of artificial amino acid sequences that fold into stable proteins with desired functions. In the current issue of Nature, two papers from the Ranganathan group (Russ et al., 2005; Socolich et al., 2005) report remarkable success in the design of artificial WW domains. Their method, termed statistical coupling analysis (Lockless and Ranganathan, 1999), does not use structural or physicochemical information but instead extracts information about essential patterns of amino acids from the evolutionary record.
Smock
Robert G
RG
Department of Biochemistry & Molecular Biology, University of Massachusetts Amherst, 01003, USA.
Gierasch
Lila M
LM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D003627:Data Interpretation, Statistical; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D015202:Protein Engineering; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D000596:Amino Acids; D011506:Proteins