2010
DOI: 10.1002/psc.1288
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Abstract: The GroEL-GroES is an essential molecular chaperon system that assists protein folding in cell. Binding of various substrate proteins to GroEL is one of the key aspects in GroEL-assisted protein folding. Small peptides may mimic segments of the substrate proteins in contact with GroEL, and allow detailed structural analysis of the interactions. A model peptide SBP has been shown to bind to a region in GroEL that is important for binding of substrate proteins. Here, we investigated whether the observed GroEL-SB… Show more

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Cited by 11 publications
(8 citation statements)
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“…Review articles and methods papers Protein interactions with other proteins Protein interactions with small ligands (including co‐factors and drugs) …”
Section: Introductionmentioning
confidence: 99%
“…Review articles and methods papers Protein interactions with other proteins Protein interactions with small ligands (including co‐factors and drugs) …”
Section: Introductionmentioning
confidence: 99%
“…Indeed, previous experiments have even suggested the formation of rather specific structure in denatured Rho at 0.4 M GdmCl (27). CypA and Rho can therefore be considered representatives of two (49). In complex with SR1, the transfer efficiency histograms of all variants of CypA and Rho are broader than those of the free denatured proteins under physiological conditions (Fig.…”
Section: The Conformation Of Denatured Cypa and Rho Free In Solutionmentioning
confidence: 79%
“…The small mismatches in the activities between the different HBx fusions and the exact GroEL amount are not surprising and can be explained considering that GroEL activity is influenced by the presence/absence of GroES and client proteins, which, in this case, may be the different HBx fusions. 35 GroEL hydrolyzes dATP as efficiently as ATP and to a lesser extent GTP, showing that all nucleotides can also be processed by the chaperone. The dependence of the hydrolytic activity on the nature of the HBx construct and the consistent trend in nucleotide preference between GroEL and the different HBx samples ( Figure 3 C) provides convincing evidence that the chaperone, and not HBx, is responsible for the (d)NTP hydrolysis.…”
Section: Resultsmentioning
confidence: 99%