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pH dependence of the hydrogen exchange in the SH 3 domain of K-spectrin
| Content Provider | Semantic Scholar |
|---|---|
| Author | Sadqi, Mourad Casares, S. Fernández Löpez-Mayorga, O. Marẗnez, J. C. Conejero-Lara, Francisco |
| Copyright Year | 2002 |
| Abstract | Using nuclear magnetic resonance we have measured the hydrogen exchange (HX) in the Src homology region 3 (SH3) domain of K-spectrin as a function of pH*. At very acidic pH* values the exchange of most residues appears to occur via global unfolding, although several residues show abnormally large Gibbs energies of exchange, suggesting the presence of some residual structure in the unfolded state. At higher pH* HX occurs mainly via local or partial unfoldings. We have been able to characterize the coupling between the electrostatic interactions in this domain and the conformational fluctuations occurring under native conditions by analyzing the dependence upon pH* of the Gibbs energy of exchange. The SH3 domain seems to be composed of a central core, which requires large structural disruptions to become exposed to the solvent, surrounded by smaller subdomains, which fluctuate independently. ß 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://hera.ugr.es/doi/15085636.pdf |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Acids DVD region code Dependence Energy, Physics Homologous Gene Homology (biology) Hydrogen Peroxide 30 MG/ML Topical Solution Interaction Resonance Scientific Publication Small Unfolding (DSP implementation) |
| Content Type | Text |
| Resource Type | Article |
