Abstract
The production of proteins capable of binding ice is one of the strategies evolved in biological organisms for survival in cold ecosystems where there is a risk of freezing. These proteins have an important ability to bind to the surface of ice, influence its growth and prevent cell damage and death. To understand the nature of interaction of such proteins with ice, it is necessary to know their structure. This study contributes to the understanding of the structural and dynamic mechanisms of action of ice-binding proteins that ensure the adaptation of organisms in critical conditions. The study of the contribution of proteins capable of binding ice to adaptation to cold conditions opens up wide opportunities in solving a number of important medical problems, including the development of effective cellular and organ cryoprotectants, as well as long-term storage of food products without loss of their consumer properties in the food industry.
REFERENCES
H. Kawahara, in Psychrophiles: From Biodiversity to Biotechnology, Ed. by R. Margesin (Springer-Verlag, Cham, 2017), pp. 237–257.
J. S. H. Lorv, D. R. Rose, and B. R. Glick, Scientifica (Cairo) 2014, 976895 (2014).
M. Bar Dolev, I. Braslavsky, and P. L. Davies, Annu. Rev. Biochem. 85, 515 (2016).
A. Białkowska, E. Majewska, A. Olczak, and A. Twarda-Clapa, Biomolecules 10 (2), 274 (2020).
A. L. DeVries and D. E. Wohlschlag, Science 163 (3871), 1073 (1969).
C.-H. C. Cheng, Curr. Opin. Genet. Development 8 (6), 715 (1998).
C. Deng, C.-H. C. Cheng, H. Ye, et al., Proc. Natl. Acad. Sci. U. S. A. 107 (50), 21593 (2010).
D. Doucet, V. K. Walker, and W. Qin, Cell. Mol. Life Sci. 66 (8), 1404 (2009).
M. Bredow and V. K. Walker, Ice-binding proteins in plants, Front. Plant Sci. 8, 2153 (2017).
G. Deng, D. W. Andrews, and R. A. Laursen, FEBS Lett. 402, 17 (1997).
W. K. Low, Q. Lin, C. Stathakis, et al., J. Biol. Chem. 276 (15), 11582 (2001).
Z. Zhao, G. Deng, Q. Lui, and R. A. Laursen, Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. 1382 (2), 177 (1998).
A. Y. Chang, V. W. Chau, J. A. Landas, and Y. Pang, JEMI 1, 22 (2017).
Technical Bulletin, ProteaseMAX(TM) Surfactant, Trypsin Enhancer (Promega Corporation, 2015).
A. Shevchenko, M. Wilm, O. Vorm, and M. Mann, Anal. Chem. 68 (5), 850 (1996).
J. Jumper, R. Evans, A. Pritzel, et al., Nature 596 (7873), 583 (2021).
A. Waterhouse, M. Bertoni, S. Bienert, et al., Nucleic Acids Res. 46 (W1), W296 (2018).
D. Case, K. Belfon, S. Ben-Shalom, et al., Amber20 (Univ. California, San Francisco, 2020).
A. W. Gotz, M. J. Williamson, D. Xu, et al., J. Chem. Theory Comput. 8 (5), 1542 (2012).
R. Salomon-Ferrer, A. W. Gotz, D. Poole, et al., J. Chem. Theory Comput. 9 (9), 3878 (2013).
Y. Khalak, B. Baumeier, and M. Karttunen, J. Chem. Phys. 149 (22), 224507 (2018).
M. Matsumoto, T. Yagasaki, and H. Tanaka, J. Comput. Chem. 39 (1), 61 (2018).
E. F. Pettersen, T. D. Goddard, and C. C. Huang, J. Comput. Chem. 25 (13), 1605 (2004).
D. R. Roe and T. E. Cheatham, J. Chem. Theory Comput. 9 (7), 3084 (2013).
B. Bogdanov and R. D. Smith, Mass Spectrom. Rev. 24 (2), 168 (2005).
G. Deng and R. A. Laursen, Biochim. Biophys. Acta 1388 (2), 305 (1998).
C. Tian, K. Kasavajhala, K. A. A. Belfon, et al., J. Chem. Theory Comput. 16 (1), 528 (2020).
C. Vega, E. Sanz, and J. L. F. Abascal, J. Chem. Phys. 122 (11), 114507 (2005).
A. S. Oude Vrielink, A. Aloi, L. L. C. Olijve, and I. K. Voets, Biointerphases 11 (1), 18906 (2016).
Funding
The research was carried out with the financial support of the Russian Science Foundation, project no. 23-24-00256.
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
CONFLICT OF INTEREST
The authors of this article declare that they have no conflicts of interest.
ETHICS APPROVAL AND CONSENT TO PARTICIPATE
This work does not contain studies involving human and animal subjects.
Additional information
Translated by E.Puchkov
Publisher’s Note.
Pleiades Publishing remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Abbreviations: MALDI-TOF, matrix-assisted laser desorption/ionization time-of-flight.
Rights and permissions
About this article
Cite this article
Oleinik, G.A., Zhdanova, P., Koval, V.V. et al. Structure of an Ice-Binding Protein from Myoxocephalus octodecemspinosus Determined by Molecular Dynamics and Based on Circular Dichroism Spectra. BIOPHYSICS 68, 513–518 (2023). https://doi.org/10.1134/S0006350923040152
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1134/S0006350923040152