Residual charge interactions in unfolded staphylococcal nuclease can be explained by the Gaussian-chain model.
The discrepancy of the pH dependence of the unfolding free energy for staphylococcal nuclease from what is expected from an idealized model for the unfolded state is accounted for by the recently developed Gaussian-chain model. Residual electrostatic effects in the unfolded state are attributed to nonspecific interactions dominated by charges close along the sequence. The dominance of nonspecific local interactions appears to be supported by some experimental evidence.
Zhou
Huan-Xiang
HX
Department of Physics, Drexel University, Philadelphia, PA 19104, USA. zhou@sb.fsu.edu
D000596:Amino Acids / Q000737:chemistry; D004563:Electrochemistry / Q000379:methods; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008836:Micrococcal Nuclease / Q000737:chemistry*; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D015233:Models, Statistical; D016011:Normal Distribution; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D055672:Static Electricity; D013816:Thermodynamics
D000596:Amino Acids; D010446:Peptide Fragments; D008836:Micrococcal Nuclease