Issue 62, 2015
From the journal:

RSC Advances

Quaternary structures of GroEL and naïve-Hsp60 chaperonins in solution: a combined SAXS-MD study†

A. Spinello,ab   M. G. Ortore,*c   F. Spinozzi,c   C. Ricci,c   G. Barone,*ab   A. Marino Gammazzaab  and  A. Palumbo Piccionello*ab  

* Corresponding authors

a Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche-STEBICEF, Universitá degli Studi di Palermo, Viale delle Scienze, Edificio 17, 90128 Palermo, Italy
E-mail: antonio.palumbopiccionello@unipa.it, giampaolo.barone@unipa.it

b Istituto EuroMediterraneo di Scienza e Tecnologia-IEMEST, Via Emerico Amari 123, 90139 Palermo, Italy

c Dipartimento DiSVA, Università Politecnica delle Marche, Via Brecce Bianche, 60131 Ancona, Italy
E-mail: m.g.ortore@univpm.it

Abstract

The quaternary structures of bacterial GroEL and human naïve-Hsp60 chaperonins in physiological conditions have been investigated by an innovative approach based on a combination of synchrotron Small Angle X-ray Scattering (SAXS) in-solution experiments and molecular dynamics (MD) simulations. Low-resolution SAXS experiments over large and highly symmetric oligomers are analyzed on the basis of the high-resolution structure of the asymmetric protein monomers, provided by MD. The results reveal remarkable differences between the solution and the crystallographic structure of GroEL and between the solution structures of GroEL and of its human homologue Hsp60.

Graphical abstract: Quaternary structures of GroEL and naïve-Hsp60 chaperonins in solution: a combined SAXS-MD study

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Article information

DOI
https://doi.org/10.1039/C5RA05144D
Article type
Paper
Submitted
23 Mar 2015
Accepted
27 May 2015
First published
27 May 2015

RSC Adv., 2015,5, 49871-49879

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Quaternary structures of GroEL and naïve-Hsp60 chaperonins in solution: a combined SAXS-MD study

A. Spinello, M. G. Ortore, F. Spinozzi, C. Ricci, G. Barone, A. M. Gammazza and A. P. Piccionello, RSC Adv., 2015, 5, 49871 DOI: 10.1039/C5RA05144D

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