title: Combinatorial protein design.
abstract: Combinatorial protein libraries permit the examination of a wide range of sequences. Such methods are being used for denovo design and to investigate the determinants of protein folding. The exponentially large number of possible sequences, however, necessitates restrictions on the diversity of sequences in a combinatorial library. Recently, progress has been made in developing theoretical tools to bias and characterize the ensemble of sequences that fold into a given structure - tools that can be applied to the design and interpretation of combinatorial experiments.
authors.affiliation: Department of Chemistry, University of Pennsylvania, 231 South 34 Street, Philadelphia 19104, USA. saven@sas.upenn.edu
authors.forename: Jeffery G
authors.initials: JG
authors.lastname: Saven
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000235:genetics; D020650:Combinatorial Chemistry Techniques / Q000379:methods*; D003628:Database Management Systems; D030562:Databases, Protein; D016247:Information Storage and Retrieval / Q000379:methods; D019151:Peptide Library; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D020539:Sequence Analysis, Protein / Q000379:methods*; D017385:Sequence Homology
chemical_list: D000596:Amino Acids; D019151:Peptide Library; D011506:Proteins