title: Direct test of the Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins.
abstract: The Gaussian-chain model for treating residual charge-charge interactions was critically tested by recent experimental pK(a) results for individual Asp, Glu, and His residues in the unfolded drkN SH3 domain. Predicted pK(a)'s were in good agreement with experiment. The clustering of Asp and Glu residues along the sequence was suggested to limit pK(a) shifts and contribute to the folding stability by destabilizing the unfolded state.
authors.affiliation: Department of Physics, Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA. hxzhou@csit.fsu.edu
authors.forename: Huan-Xiang
authors.initials: HX
authors.lastname: Zhou
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D029721:Drosophila Proteins / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D017510:Protein Folding; D055672:Static Electricity; D018909:src Homology Domains
chemical_list: D000596:Amino Acids; D029721:Drosophila Proteins; C080530:drk protein, Drosophila