title: Finding the right fold.
abstract: Using mutational analysis, three groups have compared the transition states for the folding of two pairs of homologous proteins. The results of these studies suggest that protein folding mechanisms are conserved and are defined primarily by the overall topology of the native structures, as opposed to specific details of the interactions stabilizing these structures.
authors.affiliation: Department of Biology, University of Utah, 257 South 1400 East, Salt Lake City, Utah 84112-0840, USA. goldenberg@biology.utah.edu
authors.forename: D P
authors.initials: DP
authors.lastname: Goldenberg
mesh_terms: D001665:Binding Sites; D019277:Entropy; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
chemical_list: D011506:Proteins