13 research outputs found
Dataset concerning GroEL chaperonin interaction with proteins
No full textGroEL 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
The dimeric DNA binding domain of the human papillomavirus E2 protein folds through a monomeric intermediate which cannot be native-like
No full textDenaturation of Stefin B by GuHCl, pH and Heat; Evidence for Molten Globule Intermediates
No full textRefolding of scFv mini-antibodies using size-exclusion chromatography via arginine solution layer
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