Core-directed protein design.
For various reasons, it seems sensible to redesign or design proteins from the inside out. Past approaches in this field have involved iterations of mutagenesis and characterisation to 'evolve' designs. Increasingly, combinatorial approaches are being taken to select 'fit' sequences from libraries of variant proteins. In particular, in silico methods have been used to good effect. More recently, experimental methods have been developed and improved. We are now in a position to redesign stability and function into natural protein frameworks confidently and to attempt de novo designs for more ambitious targets.
Woolfson
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DN
Centre for Biomolecular Design and Drug Development, School of Biological Sciences, University of Sussex, Falmer BN1 9QG, UK. dek@biols.susx.ac.uk
D000465:Algorithms; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics; D036022:Capsid Proteins; D020650:Combinatorial Chemistry Techniques; D019295:Computational Biology; D004268:DNA-Binding Proteins; D015195:Drug Design; D004926:Escherichia coli; D016350:Leucine Zippers / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry* / Q000235:genetics; D016601:RNA-Binding Proteins / Q000235:genetics; D014760:Viral Fusion Proteins
D001426:Bacterial Proteins; D036022:Capsid Proteins; D004268:DNA-Binding Proteins; D011506:Proteins; D016601:RNA-Binding Proteins; C054243:Rop protein, ColE1 plasmid; D014760:Viral Fusion Proteins