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Chem"},{"key":"10.1006\/jmbi.2000.4422_BIB79","doi-asserted-by":"crossref","first-page":"8246","DOI":"10.1063\/1.468195","article-title":"Folding thermodynamics and kinetics of imprinted renaturable heteropolymers","volume":"101","author":"Pande","year":"1994","journal-title":"J. Chem. Phys"},{"key":"10.1006\/jmbi.2000.4422_BIB80","doi-asserted-by":"crossref","first-page":"12976","DOI":"10.1073\/pnas.91.26.12976","article-title":"Thermodynamic procedure to synthesize heteropolymers that can renature to recognize a given target molecule","volume":"91","author":"Pande","year":"1994","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1006\/jmbi.2000.4422_BIB81","series-title":"Statistical Mechanics","author":"Pathria","year":"1996"},{"key":"10.1006\/jmbi.2000.4422_BIB82","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/0022-2836(87)90358-5","article-title":"Tertiary templates for proteins","volume":"193","author":"Ponder","year":"1987","journal-title":"J. Mol. 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E"},{"key":"10.1006\/jmbi.2000.4422_BIB86","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1126\/science.3388019","article-title":"Combinatorial cassette mutagenesis as a probe of the informational contetn of protein sequences","volume":"241","author":"Reidhaar Olson","year":"1988","journal-title":"Science"},{"key":"10.1006\/jmbi.2000.4422_BIB87","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1093\/protein\/5.7.625","article-title":"A new approach to the design of a sequence with the highest affinity for a molecular surface","volume":"5","author":"Reva","year":"1992","journal-title":"Protein Eng"},{"key":"10.1006\/jmbi.2000.4422_BIB88","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1146\/annurev.bb.06.060177.001055","article-title":"Areas, volumes, packing, and protein structure","volume":"6","author":"Richards","year":"1977","journal-title":"Annu. Rev. Biophys. 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B"},{"key":"10.1006\/jmbi.2000.4422_BIB95","doi-asserted-by":"crossref","first-page":"3373","DOI":"10.1021\/bi9625758","article-title":"Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L","volume":"36","author":"Scalley","year":"1997","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2000.4422_BIB96","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1038\/nsb1297-1039","article-title":"A designed four-helix bundle protein with native-like structure","volume":"4","author":"Schafmeister","year":"1997","journal-title":"Nature Struct. Biol"},{"key":"10.1006\/jmbi.2000.4422_BIB97","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1006\/jmbi.1993.1172","article-title":"Rotamers","volume":"230","author":"Schrauber","year":"1993","journal-title":"J. Mol. 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