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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hoatson, Gina L. Vugmeyster, Liliya Penland, Kirsten Vold, Robert L. Ostrovsky, Dmitry |
| Description | Author Affiliation: Vugmeyster L ( Department of Chemistry, University of Alaska Anchorage, Anchorage, Alaska 99508, USA. lvugmeyster@uaa.alaska.edu) |
| Abstract | We investigated site-specific dynamics of key methyl groups in the hydrophobic core of chicken villin headpiece subdomain (HP36) over the temperature range between 298 and 140 K using deuteron solid-state NMR longitudinal relaxation measurements. The relaxation of the longitudinal magnetization is weakly nonexponential (glassy) at high temperatures and exhibits a stronger degree of nonexponentiality below about 175 K. In addition, the characteristic relaxation times deviate from the simple Arrhenius law. We interpret this behavior via the existence of distribution of activation energy barriers for the three-site methyl jumps, which originates from somewhat different methyl environments within the local energy landscape. The width of the distribution of the activation barriers for methyl jumps is rather significant, about 1.4 kJ/mol. Our experimental results and modeling allow for the description of the apparent change at about 175 K without invoking a specific transition temperature. For most residues in the core, the relaxation behavior at high temperatures points to the existence of conformational exchange between the substates of the landscape, and our model takes into account the kinetics of this process. The observed dynamics are the same for dry and hydrated protein. We also looked at the effect of F58L mutation inside the hydrophobic core on the dynamics of one of the residues and observed a significant increase in its conformational exchange rate constant at high temperatures. |
| ISSN | 15206106 |
| e-ISSN | 15205207 |
| Journal | The Journal of Physical Chemistry B |
| Issue Number | 4 |
| Volume Number | 117 |
| Language | English |
| Publisher | American Chemical Society (United States) |
| Publisher Date | 2013-01-31 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Neurofilament Proteins Chemistry Nuclear Magnetic Resonance, Biomolecular Peptide Fragments Thermodynamics Animals Hydrophobic And Hydrophilic Interactions Temperature Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Physical chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Surfaces, Coatings and Films Materials Chemistry Medicine Physical and Theoretical Chemistry |
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