ArticleProtein science : a publication of the Protein Society2012
Thermal coefficients of the methyl groups within ubiquitin.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 25 citations in OpenAlex.
- Early Divergence in Misfolding Pathways of Amyloid-Beta Peptides.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
- Optimal design of adaptively sampled NMR experiments for measurement of methyl group dynamics with application to a ribosome-nascent chain complex.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2021Article
- Enhancing NMR derived ensembles with kinetics on multiple timescales.Journal of biomolecular NMR · 2020Article
- Functional Role of Solvent Entropy and Conformational Entropy of Metal Binding in a Dynamically Driven Allosteric System.Journal of the American Chemical Society · 2018Article
- Entropy in molecular recognition by proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Flexibility and Solvation of Amyloid-β Hydrophobic Core.The Journal of biological chemistry · 2016Article
- The unusual internal motion of the villin headpiece subdomain.Protein science : a publication of the Protein Society · 2016Article
- Structural Integrity of the A147T Polymorph of Mammalian TSPO.Chembiochem : a European journal of chemical biology · 2015Article
- Dynamic multidrug recognition by multidrug transcriptional repressor LmrR.Scientific reports · 2014Article
- Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein.Protein science : a publication of the Protein Society · 2014Article
- Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.Molecules (Basel, Switzerland) · 2013Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Physiological processes such as protein folding and molecular recognition are intricately linked to their dynamic signature, which is reflected in their thermal coefficient. In addition, the local conformational entropy is directly related to the degrees of freedom, which each residue possesses within its conformational space. Therefore, the temperature dependence of the local conformational entropy may provide insight into understanding how local dynamics may affect the stability of proteins. Here, we analyze the temperature dependence of internal methyl group dynamics derived from the cross-correlated relaxation between dipolar couplings of two CH bonds within ubiquitin. Spanning a temperature range from 275 to 308 K, internal methyl group dynamics tend to increase with increasing temperature, which translates to a general increase in local conformational entropy. With this data measured over multiple temperatures, the thermal coefficient of the methyl group order parameter, the characteristic thermal coefficient, and the local heat capacity were obtained. By analyzing the distribution of methyl group thermal coefficients within ubiquitin, we found that the N-terminal region has relatively high thermostability. These results indicate that methyl groups contribute quite appreciably to the total heat capacity of ubiquitin through the regulation of local conformational entropy.
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