FEBS Letters
Volume 583, Issue 6 , Pages 953-959, 18 March 2009

Insight into “insoluble proteins” with pure water

Edited by Peter Brzezinski

  • Jianxing Song

      Affiliations

    • Corresponding Author InformationAddress: Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore. Fax: +65 67792486.

Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore

Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore

Received 27 January 2009; received in revised form 14 February 2009; accepted 16 February 2009. published online 23 February 2009.

Abstract 

Many proteins are not refoldable and also insoluble. Previously no general method was available to solubilize them and consequently their structural properties remained unknown. Surprisingly, we recently discovered that all insoluble proteins in our laboratory, which are highly diverse, can be solubilized in pure water. Structural characterization by CD and NMR led to their classification into three groups, all of which appear trapped in the highly disordered or partially-folded states with a substantial exposure of hydrophobic side chains. In this review, I discuss our results in a wide context and subsequently propose a model to rationalize the discovery. The potential applications are also explored in studying protein folding, design and membrane proteins.

Keywords: Water, Insoluble protein, Protein folding, Protein solubility, Ionic strength, Circular dichroism (CD), NMR

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PII: S0014-5793(09)00133-1

doi:10.1016/j.febslet.2009.02.022

FEBS Letters
Volume 583, Issue 6 , Pages 953-959, 18 March 2009

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