Dataset concerning GroEL chaperonin interaction with proteins

GroEL chaperonin is well-known to interact with a wide variety of polypeptide chains. Here we show the data related to our previous work (http://dx.doi.org/10.1016/j.pep.2015.11.020[1]), and concerning the interaction of GroEL with native (lysozyme, α-lactalbumin) and denatured (lysozyme, α-lactalbu...

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Bibliographic Details
Published in:	Data in brief Vol. 6; pp. 619 - 624
Main Authors:	Marchenkov, V.V., Marchenko, N.Yu, Kaysheva, A.L., Kotova, N.V., Kashparov, I.A., Semisotnov, G.V.
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier Inc 01-03-2016 Elsevier
Subjects:	Data
Online Access:	Get full text
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Summary:	GroEL chaperonin is well-known to interact with a wide variety of polypeptide chains. Here we show the data related to our previous work (http://dx.doi.org/10.1016/j.pep.2015.11.020[1]), and concerning the interaction of GroEL with native (lysozyme, α-lactalbumin) and denatured (lysozyme, α-lactalbumin and pepsin) proteins in solution. The use of affinity chromatography on the base of denatured pepsin for GroEL purification from fluorescent impurities is represented as well.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	2352-3409 2352-3409
DOI:	10.1016/j.dib.2016.01.008