Standard

Determination the structure of an ice-bindingprotein from the fish Myoxocephalusoctodecemspinosus by circular dichroism andHDX-MS methods. / Oleinik, Galina A.; Baranova, Svetlana V.; Zhdanova, Polina V. и др.

в: FEBS Open Bio, Том 13, № S2, P-06.1-14, 2023, стр. 174.

Результаты исследований: Научные публикации в периодических изданияхстатья по материалам конференцииРецензирование

Harvard

Oleinik, GA, Baranova, SV, Zhdanova, PV, Chernonosov, AA & Коваль, ВВ 2023, 'Determination the structure of an ice-bindingprotein from the fish Myoxocephalusoctodecemspinosus by circular dichroism andHDX-MS methods', FEBS Open Bio, Том. 13, № S2, P-06.1-14, стр. 174.

APA

Oleinik, G. A., Baranova, S. V., Zhdanova, P. V., Chernonosov, A. A., & Коваль, В. В. (2023). Determination the structure of an ice-bindingprotein from the fish Myoxocephalusoctodecemspinosus by circular dichroism andHDX-MS methods. FEBS Open Bio, 13(S2), 174. [P-06.1-14].

Vancouver

Author

Oleinik, Galina A. ; Baranova, Svetlana V. ; Zhdanova, Polina V. и др. / Determination the structure of an ice-bindingprotein from the fish Myoxocephalusoctodecemspinosus by circular dichroism andHDX-MS methods. в: FEBS Open Bio. 2023 ; Том 13, № S2. стр. 174.

BibTeX

@article{b2c1ffa6b51f4439afd266bebfd90e8b,
title = "Determination the structure of an ice-bindingprotein from the fish Myoxocephalusoctodecemspinosus by circular dichroism andHDX-MS methods",
abstract = "At the various low temperatures areas of our planet, a numberof organisms survive due to the ice-binding proteins (IBPs).These proteins can bind to ice crystals and affect their growth invarious ways to prevent cell damage and death. These proteinscould be used in various fields of human activity such as medi-cine, agriculture, food industry. For example, they are useful topreserve the quality of products during freezing. In medicine,IBPs could be used as cryoprotectants during the transportationof organs. For optimal use of IBPs proteins, we should under-stand the binding mechanisms, and know their structure. Wechose a representative class IV ice-binding proteins as the objectof study in this work. This protein was found in the fish speciesMyoxocephalus octodecemspinosus (P809061). To present thestructure of the studied protein has not been determined in apractical way. To determine the IBP structure, we used the circu-lar dichroism and HDX-MS methods. The advantage of thesemethods is that they allow the study of protein in solution,require a small amount of sample, the size of the protein has norestrictions, and the reliability of the results obtained is proven.The obtained data allow us to clarify the secondary structure ofclass IV protein P809061 and give an idea of the binding mecha-nisms to ice crystals. This work was supported by the RussianScience Foundation 23-24-00256 and Russian Ministry of HigherEducation and Science 075-15-2022-263. *The authors markedwith an asterisk equally contributed to the work.",
author = "Oleinik, {Galina A.} and Baranova, {Svetlana V.} and Zhdanova, {Polina V.} and Chernonosov, {Alexander A.} and Коваль, {Владимир Васильевич}",
year = "2023",
language = "English",
volume = "13",
pages = "174",
journal = "FEBS Open Bio",
issn = "2211-5463",
publisher = "John Wiley & Sons Inc.",
number = "S2",

}

RIS

TY - JOUR

T1 - Determination the structure of an ice-bindingprotein from the fish Myoxocephalusoctodecemspinosus by circular dichroism andHDX-MS methods

AU - Oleinik, Galina A.

AU - Baranova, Svetlana V.

AU - Zhdanova, Polina V.

AU - Chernonosov, Alexander A.

AU - Коваль, Владимир Васильевич

PY - 2023

Y1 - 2023

N2 - At the various low temperatures areas of our planet, a numberof organisms survive due to the ice-binding proteins (IBPs).These proteins can bind to ice crystals and affect their growth invarious ways to prevent cell damage and death. These proteinscould be used in various fields of human activity such as medi-cine, agriculture, food industry. For example, they are useful topreserve the quality of products during freezing. In medicine,IBPs could be used as cryoprotectants during the transportationof organs. For optimal use of IBPs proteins, we should under-stand the binding mechanisms, and know their structure. Wechose a representative class IV ice-binding proteins as the objectof study in this work. This protein was found in the fish speciesMyoxocephalus octodecemspinosus (P809061). To present thestructure of the studied protein has not been determined in apractical way. To determine the IBP structure, we used the circu-lar dichroism and HDX-MS methods. The advantage of thesemethods is that they allow the study of protein in solution,require a small amount of sample, the size of the protein has norestrictions, and the reliability of the results obtained is proven.The obtained data allow us to clarify the secondary structure ofclass IV protein P809061 and give an idea of the binding mecha-nisms to ice crystals. This work was supported by the RussianScience Foundation 23-24-00256 and Russian Ministry of HigherEducation and Science 075-15-2022-263. *The authors markedwith an asterisk equally contributed to the work.

AB - At the various low temperatures areas of our planet, a numberof organisms survive due to the ice-binding proteins (IBPs).These proteins can bind to ice crystals and affect their growth invarious ways to prevent cell damage and death. These proteinscould be used in various fields of human activity such as medi-cine, agriculture, food industry. For example, they are useful topreserve the quality of products during freezing. In medicine,IBPs could be used as cryoprotectants during the transportationof organs. For optimal use of IBPs proteins, we should under-stand the binding mechanisms, and know their structure. Wechose a representative class IV ice-binding proteins as the objectof study in this work. This protein was found in the fish speciesMyoxocephalus octodecemspinosus (P809061). To present thestructure of the studied protein has not been determined in apractical way. To determine the IBP structure, we used the circu-lar dichroism and HDX-MS methods. The advantage of thesemethods is that they allow the study of protein in solution,require a small amount of sample, the size of the protein has norestrictions, and the reliability of the results obtained is proven.The obtained data allow us to clarify the secondary structure ofclass IV protein P809061 and give an idea of the binding mecha-nisms to ice crystals. This work was supported by the RussianScience Foundation 23-24-00256 and Russian Ministry of HigherEducation and Science 075-15-2022-263. *The authors markedwith an asterisk equally contributed to the work.

UR - https://febs.onlinelibrary.wiley.com/doi/epdf/10.1002/2211-5463.13646

M3 - Conference article

VL - 13

SP - 174

JO - FEBS Open Bio

JF - FEBS Open Bio

SN - 2211-5463

IS - S2

M1 - P-06.1-14

ER -

ID: 71520334