Dataset concerning GroEL chaperonin interaction with proteins
V.V. Marchenkov,
N.Yu. Marchenko,
A.L. Kaysheva,
N.V. Kotova,
I.A. Kashparov,
G.V. Semisotnov
Affiliations
V.V. Marchenkov
Institute of Protein Research, RAS, Russia
N.Yu. Marchenko
Institute of Protein Research, RAS, Russia
A.L. Kaysheva
Institute of Protein Research, RAS, Russia
N.V. Kotova
Institute of Protein Research, RAS, Russia
I.A. Kashparov
Institute of Protein Research, RAS, Russia
G.V. Semisotnov
Corresponding author at: Institute of Protein Research RAS, 142290, Pushchino, Moscow Region, Russia. Tel./ fax: +7 495 514 02 18.; Institute of Protein Research, RAS, Russia
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.
