Protein folding from a combinatorial perspective.
Combinatorial mutagenesis experiments show the existence of many different solutions to the problem of complementary packing of non-polar sidechains in the protein core. They suggest that a significant amount of structural information is carried by the simple pattern of polar and non-polar residues along the polypeptide chain, indicate that the formation of buried polar interactions may be a fundamentally slow step in protein folding and show that proteins with many native properties occur at reasonable frequencies in random sequence libraries.
Sauer
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Department of Biology, Massachusetts Institute of Technology, Cambridge 02139-4307, USA. bobsauer@mit.edu
D004268:DNA-Binding Proteins; D006860:Hydrogen Bonding; D015394:Molecular Structure; D016296:Mutagenesis; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics; D054334:Viral Regulatory and Accessory Proteins
D004268:DNA-Binding Proteins; D011506:Proteins; D012097:Repressor Proteins; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins