KFU. Card publication. Statistical prediction of protein structural, localization and functional properties by the analysis of its fragment mass distributions after proteolytic cleavage

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STATISTICAL PREDICTION OF PROTEIN STRUCTURAL, LOCALIZATION AND FUNCTIONAL PROPERTIES BY THE ANALYSIS OF ITS FRAGMENT MASS DISTRIBUTIONS AFTER PROTEOLYTIC CLEAVAGE

Form of presentation

Articles in international journals and collections

Year of publication

2016

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Authors, employees of KFU

Kayumov Ayrat Rashitovich, author

Other authors

Bunde Armin -, author

Bogachev Mikhail Igorevich, author

Markelov Oleg A., author

Bibliographic description in the original language

Bogachev, M. Statistical prediction of protein structural, localization and functional properties by the analysis of its fragment mass distributions after proteolytic cleavage / M. Bogachev, A.R. Kayumov, O. Markelov, Armin Bunde // SCIENTIFIC REPORTS. - 2016. - V.6.

Annotation

Structural, localization and functional properties of unknown proteins are often being predicted from their primary polypeptide chains using sequence alignment with already characterized proteins and consequent molecular modeling. Here we suggest an approach to predict various structural and structure-associated properties of proteins directly from the mass distributions of their proteolytic cleavage fragments. For amino-acid-specific cleavages, the distributions of fragment masses are determined by the distributions of inter-amino-acid intervals in the protein, that in turn apparently reflect its structural and structure-related features. Large-scale computer simulations revealed that for transmembrane proteins, either α-helical or β -barrel secondary structure could be predicted with about 90% accuracy after thermolysin cleavage. Moreover, 3/4 intrinsically disordered proteins could be correctly distinguished from proteins with fixed three-dimensional structure belonging to all four

Keywords

The name of the journal

SCIENTIFIC REPORTS

URL

http://www.nature.com/articles/srep22286

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=127895&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Kayumov Ayrat Rashitovich	ru_RU
dc.contributor.author	Bunde Armin -	ru_RU
dc.contributor.author	Bogachev Mikhail Igorevich	ru_RU
dc.contributor.author	Markelov Oleg A.	ru_RU
dc.date.accessioned	2016-01-01T00:00:00Z	ru_RU
dc.date.available	2016-01-01T00:00:00Z	ru_RU
dc.date.issued	2016	ru_RU
dc.identifier.citation	Bogachev, M. Statistical prediction of protein structural, localization and functional properties by the analysis of its fragment mass distributions after proteolytic cleavage / M. Bogachev, A.R. Kayumov, O. Markelov, Armin Bunde // SCIENTIFIC REPORTS. - 2016. - V.6.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=127895&p_lang=2	ru_RU
dc.description.abstract	SCIENTIFIC REPORTS	ru_RU
dc.description.abstract	Structural, localization and functional properties of unknown proteins are often being predicted from their primary polypeptide chains using sequence alignment with already characterized proteins and consequent molecular modeling. Here we suggest an approach to predict various structural and structure-associated properties of proteins directly from the mass distributions of their proteolytic cleavage fragments. For amino-acid-specific cleavages, the distributions of fragment masses are determined by the distributions of inter-amino-acid intervals in the protein, that in turn apparently reflect its structural and structure-related features. Large-scale computer simulations revealed that for transmembrane proteins, either α-helical or β -barrel secondary structure could be predicted with about 90% accuracy after thermolysin cleavage. Moreover, 3/4 intrinsically disordered proteins could be correctly distinguished from proteins with fixed three-dimensional structure belonging to all four	ru_RU
dc.language.iso	ru	ru_RU
dc.subject		ru_RU
dc.title	Statistical prediction of protein structural, localization and functional properties by the analysis of its fragment mass distributions after proteolytic cleavage	ru_RU
dc.type	Articles in international journals and collections	ru_RU