ArticleThe journal of physical chemistry. B2015
Complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments.
Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Ligand entry in human ileal bile acid-binding protein is mediated by histidine protonation.Scientific reports · 2019Article
- Applications of NMR and computational methodologies to study protein dynamics.Archives of biochemistry and biophysics · 2017Review
- Networks of Dynamic Allostery Regulate Enzyme Function.Structure (London, England : 1993) · 2017Article
- Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds.Microbial cell factories · 2016Article
- Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function.Progress in nuclear magnetic resonance spectroscopy · 2016Review
- Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme Activity.Structure (London, England : 1993) · 2015Article
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Abstract
The millisecond time scale motions in ribonuclease A (RNase A) were studied by solution NMR CPMG and off-resonance R1ρ relaxation dispersion experiments over a wide pH and temperature range. These experiments identify three separate protein regions termed Cluster 1, Cluster 2, and R33, whose motions are governed by distinct thermodynamic parameters. Moreover, each of these regions has motions with different pH dependencies. Cluster 1 shows an increase in activation enthalpy and activation entropy as the pH is lowered, whereas Cluster 2 exhibits the opposite behavior. In contrast, the activation enthalpy and entropy of R33 show no pH dependence. Compounding the differences, Δω values for Cluster 2 are characteristic of two-site conformational exchange, yet similar analysis for Cluster 1 indicates that this region of the enzyme exhibits conformational fluctuations between a major conformer and a pH-dependent average of protonated and deprotonated minor conformers.
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