title: The protein folding transition state: what are Phi-values really telling us?
abstract: Protein engineering-based studies of the folding transition state have accelerated significantly in the last decade, and more than a half dozen proteins have been subjected to extensive Phi-value analysis. A general picture is emerging from these studies of a transition state in which the large majority of experimentally characterized side chains participate in relatively homogeneous and energetically weak interactions playing only a relatively small role in defining relative folding rates.
authors.affiliation: Department of Chemistry, Graduate Program in Biochemistry and Structural Biology, State University of New York at Stony Brook, NY 11794-3400, USA.
authors.forename: Daniel P
authors.initials: DP
authors.lastname: Raleigh
authors.forename: Kevin W
authors.initials: KW
authors.lastname: Plaxco
mesh_terms: D011487:Protein Conformation; D015202:Protein Engineering; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D011506:Proteins