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Probing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880

Title
Probing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880
Authors
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
2016-01-14
Citation
PLoS ONE, 11(1)
Type
Article
Article Type
Article
Keywords
Bacterial ProteinCircular DichroismFluorescence AnalysisGuanidineHydrophobicityMathematical ComputingMethanothermobacter ThermautotrophicusMolecular DynamicsMolecular ModelMolecular ProbeMTH1880 ProteinNon-HumanNuclear Magnetic ResonanceProtein DenaturationProtein FoldingProtein ModificationProtein RefoldingProtein StabilityProtein StructureProtein UnfoldingSize Exclusion ChromatographySpectroscopyStatic ElectricityThermal ExposureThermodynamicsThermophilic ProteinUnclassified DrugUrea
ISSN
1932-6203
Abstract
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.
URI
http://hdl.handle.net/20.500.11750/2739
DOI
10.1371/journal.pone.0145853
Publisher
Public Library of Science
Related Researcher
  • Author Chang, Ik Soo Theoretical and Computational Biophysics Laboratory
  • Research Interests
Files:
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Collection:
Brain and Cognitive SciencesTheoretical and Computational Biophysics Laboratory1. Journal Articles
Brain and Cognitive SciencesETC1. Journal Articles


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