TITLE

Protecting role of cosolvents in protein denaturation by SDS: a structural study

AUTHOR(S)
Michaux, Catherine; Pouyez, Jenny; Wouters, Johan; Privé, Gilbert G.
PUB. DATE
January 2008
SOURCE
BMC Structural Biology;2008, Vol. 8, Special section p1
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Background: Recently, we reported a unique approach to preserve the activity of some proteins in the presence of the denaturing agent, Sodium Dodecyl Sulfate (SDS). This was made possible by addition of the amphipathic solvent 2,4-Methyl-2-PentaneDiol (MPD), used as protecting but also as refolding agent for these proteins. Although the persistence of the protein activity in the SDS/ MPD mixture was clearly established, preservation of their structure was only speculative until now. Results: In this paper, a detailed X-ray study addresses the pending question. Crystals of hen egg-white lysozyme were grown for the first time in the presence of MPD and denaturing concentrations of SDS. Depending on crystallization conditions, tetragonal crystals in complex with either SDS or MPD were collected. The conformation of both structures was very similar to the native lysozyme and the obtained complexes of SDS-lysozyme and MPD-lysozyme give some insights in the interplay of protein-SDS and protein-MPD interactions. Conclusion: This study clearly established the preservation of the enzyme structure in a SDS/MPD mixture. It is hypothesized that high concentrations of MPD would change the properties of SDS and lower or avoid interactions between the denaturant and the protein. These structural data therefore support the hypothesis that MPD avoids disruption of the enzyme structure by SDS and can protect proteins from SDS denaturation.
ACCESSION #
35702896

 

Related Articles

  • Role of N-methyl-8-(alkoxy)quinolinium iodide in suppression of protein-protein interactions. OJHA, BIMLESH; KAR, CHIRANTAN; DAS, GOPAL // Journal of Chemical Sciences;Mar2013, Vol. 125 Issue 2, p229 

    There is a great deal of interest in developing small molecule inhibitors of protein misfolding and aggregation due to a growing number of pathologic states known as amyloid disorders. In searching for alternative ways to reduce protein-protein interactions or to inhibit the amyloid formation,...

  • From A to B: A ride in the free energy surfaces of protein G domains suggests how new folds arise. Sutto, Ludovico; Camilloni, Carlo // Journal of Chemical Physics;5/14/2012, Vol. 136 Issue 18, p185101 

    Metamorphic proteins are an extremely intriguing case of protein evolution and a golden opportunity to challenge the current simplified models. In a recent work, we showed that a coarse-grained Gō model can be used to study the thermodynamics of lymphotactin, a naturally occurring metamorphic...

  • Theoretical aspects of pressure and solute denaturation of proteins: A Kirkwood-buff-theory approach. Ben-Naim, Arieh // Journal of Chemical Physics;12/21/2012, Vol. 137 Issue 23, p235102 

    A new approach to the problem of pressure-denaturation (PD) and solute-denaturation (SD) of proteins is presented. The problem is formulated in terms of Le Chatelier principle, and a solution is sought in terms of the Kirkwood-Buff theory of solutions. It is found that both problems have one...

  • Trapped in the act. Baker, Tania A. // Nature;9/2/1999, Vol. 401 Issue 6748, p29 

    Comments on the paper `Global Unfolding of a Substrate Protein by the Hsp100 Chaperone ClpA,' by Eilika U. Weber-Ban, Brian G. Reid, et al, published in the September 2, 1999, issue of the `Nature' magazine. Protein unfolding of Clp/Hsp100 family of proteins; Protein folding.

  • Distribution, Transition and Thermodynamic Stability of Protein Conformations in the Denaturant-Induced Unfolding of Proteins. Bian, Liujiao; Ji, Xu // PLoS ONE;Mar2014, Vol. 9 Issue 3, p1 

    Background: Extensive and intensive studies on the unfolding of proteins require appropriate theoretical model and parameter to clearly illustrate the feature and characteristic of the unfolding system. Over the past several decades, four approaches have been proposed to describe the interaction...

  • Reversible dioxygen binding in solvent-free liquid myoglobin. Perriman, Adam W.; Brogan, Alex P. S.; Cölfen, Helmut; Tsoureas, Nikolaos; Owen, Gareth R.; Mann, Stephen // Nature Chemistry;Aug2010, Vol. 2 Issue 8, p622 

    The ensemble of forces that stabilize protein structure and facilitate biological function are intimately linked with the ubiquitous aqueous environment of living systems. As a consequence, biomolecular activity is highly sensitive to the interplay of solvent–protein interactions, and...

  • Solvent Viscosity and Friction in Protein Folding Dynamics. Hagen, Stephen J. // Current Protein & Peptide Science;Aug2010, Vol. 11 Issue 5, p385 

    No abstract available.

  • Multi-Scaled Explorations of Binding-Induced Folding of Intrinsically Disordered Protein Inhibitor IA3 to its Target Enzyme. Jin Wang; Yong Wang; Xiakun Chu; Hagen, Stephen J.; Wei Han; Erkang Wang // PLoS Computational Biology;Apr2011, Vol. 7 Issue 4, p1 

    Biomolecular function is realized by recognition, and increasing evidence shows that recognition is determined not only by structure but also by flexibility and dynamics. We explored a biomolecular recognition process that involves a major conformational change - protein folding. In particular,...

  • Theory of cold denaturation of proteins. Ben-Naim, Arieh // Advances in Biological Chemistry;Feb2013, Vol. 3 Issue 1, p29 

    A new approach to the problem of cold denaturation is presented. It is based on solvent-induced effects operating on hydrophilic groups along the protein. These effects are stronger than the corresponding hydrophobic effects, and they operate on the hydrophilic groups which are plentiful than...

Share

Read the Article

Courtesy of VIRGINIA BEACH PUBLIC LIBRARY AND SYSTEM

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics