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Stavros P, Malecki PH, Theodoridou M, et al. The stability of the TIM-barrel domain of a psychrophilic chitinase. Biochem Biophys Rep. 2015;3:108-116doi: 10.1016/j.bbrep.2015.07.016.
Stavros, P., Malecki, P. H., Theodoridou, M., Rypniewski, W., Vorgias, C. E., & Nounesis, G. (2015). The stability of the TIM-barrel domain of a psychrophilic chitinase. Biochemistry and biophysics reports, 3108-116. https://doi.org/10.1016/j.bbrep.2015.07.016
Stavros, Philemon, et al. "The stability of the TIM-barrel domain of a psychrophilic chitinase." Biochemistry and biophysics reports vol. 3 (2015): 108-116. doi: https://doi.org/10.1016/j.bbrep.2015.07.016
Stavros P, Malecki PH, Theodoridou M, Rypniewski W, Vorgias CE, Nounesis G. The stability of the TIM-barrel domain of a psychrophilic chitinase. Biochem Biophys Rep. 2015 Jul 30;3:108-116. doi: 10.1016/j.bbrep.2015.07.016. eCollection 2015 Sep. PMID: 29124173; PMCID: PMC5668695.
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Biochem Biophys Rep. 2015 Jul 30;3:108-116. doi: 10.1016/j.bbrep.2015.07.016. eCollection 2015 Sep.

The stability of the TIM-barrel domain of a psychrophilic chitinase.

Biochemistry and biophysics reports

Philemon Stavros, Piotr H Malecki, Maria Theodoridou, Wojciech Rypniewski, Constantinos E Vorgias, George Nounesis

Affiliations

  1. Biomolecular Physics Laboratory, INRASTES, National Centre for Scientific Research "Demokritos", 153 10 Aghia Paraskevi, Greece.
  2. Physics Department, National and Kapodistrian University of Athens, 157 01 Zografou, Greece.
  3. Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznan, Poland.
  4. Department of Biochemistry and Molecular Biology, National and Kapodistrian University of Athens, 157 01 Zografou, Greece.

PMID: 29124173 PMCID: PMC5668695 DOI: 10.1016/j.bbrep.2015.07.016

Abstract

Chitinase 60 from the psychrophilic bacterium Moritella marina (MmChi60) is a four-domain protein whose structure revealed flexible hinge regions between the domains, yielding conformations in solution that range from fully extended to compact. The catalytic domain is a shallow-grooved TIM-barrel. Heat-induced denaturation experiments of the wild-type and mutants resulting from the deletions of the two-Ig-like domains and the chitin binding domain reveal calorimetric profiles that are consistent with non-collaborative thermal unfolding of the individual domains, a property that must be associated to the "hinge-regions". The calorimetric measurements of the (

Keywords: Calorimetry; Chemical denaturation; Psychrophilic TIM-barrel; Stability; Thermodynamics; Unfolding

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