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Probing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880
- Probing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880
- Kim, H[Kim, Heeyoun]; Kim, S[Kim, Sangyeol]; Jung, Y[Jung, Youngjin]; Han, J[Han, Jeongmin]; Yun, JH[Yun, Ji-Hye]; Chang, I[Chang, Iksoo]; Lee, W[Lee, Weontae]
- DGIST Authors
- Kim, S[Kim, Sangyeol]; Chang, I[Chang, Iksoo]
- Issue Date
- PLoS ONE, 11(1)
- Article Type
- Bacterial Protein; Circular Dichroism; Fluorescence Analysis; Guanidine; Hydrophobicity; Mathematical Computing; Methanothermobacter Thermautotrophicus; Molecular Dynamics; Molecular Model; Molecular Probe; MTH1880 Protein; Non-Human; Nuclear Magnetic Resonance; Protein Denaturation; Protein Folding; Protein Modification; Protein Refolding; Protein Stability; Protein Structure; Protein Unfolding; Size Exclusion Chromatography; Spectroscopy; Static Electricity; Thermal Exposure; Thermodynamics; Thermophilic Protein; Unclassified Drug; Urea
- The folding mechanism of typical proteins has been studied widely, while our understanding of the origin of the high stability of thermophilic proteins is still elusive. Of particular interest is how an atypical thermophilic protein with a novel fold maintains its structure and stability under extreme conditions. Folding-unfolding transitions of MTH1880, a thermophilic protein from Methanobacterium thermoautotrophicum, induced by heat, urea, and GdnHCl, were investigated using spectroscopic techniques including circular dichorism, fluorescence, NMR combined with molecular dynamics (MD) simulations. Our results suggest that MTH1880 undergoes a two-state N to D transition and it is extremely stable against temperature and denaturants. The reversibility of refolding was confirmed by spectroscopic methods and size exclusion chromatography. We found that the hyper-stability of the thermophilic MTH1880 protein originates from an extensive network of both electrostatic and hydrophobic interactions coordinated by the central β-sheet. Spectroscopic measurements, in combination with computational simulations, have helped to clarify the thermodynamic and structural basis for hyper-stability of the novel thermophilic protein MTH1880. © 2016 Kim et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
- Public Library of Science
- Related Researcher
Chang, Ik Soo
Theoretical and Computational Biophysics Laboratory
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