ArticlePloS one2016
Probing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880.
Article in PloS one, 2016. 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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Who cites it
6 citing papers in PubMed.
- Structure and stability of an apo thermophilic esterase that hydrolyzes polyhydroxybutyrate.Acta crystallographica. Section D, Structural biology · 2024Article
- The Wako-Saitô-Muñoz-Eaton Model for Predicting Protein Folding and Dynamics.Molecules (Basel, Switzerland) · 2022Review
- Computational design of a thermolabile uracil-DNA glycosylase of Escherichia coli.Biophysical journal · 2022Article
- Evolution of Protein Structure and Stability in Global Warming.International journal of molecular sciences · 2020Review
- Thermophilic Proteins as Versatile Scaffolds for Protein Engineering.Microorganisms · 2018Review
- CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation.Scientific reports · 2018Article
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Authors and funding
7 authors.
Funding
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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.
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