Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.febslet.2009.02.022
Title: Insight into "insoluble proteins" with pure water
Authors: Song, J. 
Keywords: Circular dichroism (CD)
Insoluble protein
Ionic strength
NMR
Protein folding
Protein solubility
Water
Issue Date: 2009
Source: Song, J. (2009). Insight into "insoluble proteins" with pure water. FEBS Letters 583 (6) : 953-959. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2009.02.022
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. © 2009 Federation of European Biochemical Societies.
Source Title: FEBS Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/28714
ISSN: 00145793
DOI: 10.1016/j.febslet.2009.02.022
Appears in Collections:Staff Publications

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