Insight into "insoluble proteins" with pure water
- PMID: 19233178
- DOI: 10.1016/j.febslet.2009.02.022
Insight into "insoluble proteins" with pure water
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.
Similar articles
-
Resurrecting abandoned proteins with pure water: CD and NMR studies of protein fragments solubilized in salt-free water.Biophys J. 2006 Dec 1;91(11):4201-9. doi: 10.1529/biophysj.106.093187. Epub 2006 Sep 15. Biophys J. 2006. PMID: 16980357 Free PMC article.
-
Insoluble protein characterization by circular dichroism (CD) spectroscopy and nuclear magnetic resonance (NMR).Methods Mol Biol. 2015;1258:371-85. doi: 10.1007/978-1-4939-2205-5_21. Methods Mol Biol. 2015. PMID: 25447876 Review.
-
Structural interpretation of paramagnetic relaxation enhancement-derived distances for disordered protein states.J Mol Biol. 2009 Jul 17;390(3):467-77. doi: 10.1016/j.jmb.2009.05.019. Epub 2009 May 15. J Mol Biol. 2009. PMID: 19447112
-
Dissecting entropic coiling and poor solvent effects in protein collapse.J Am Chem Soc. 2008 Sep 3;130(35):11578-9. doi: 10.1021/ja802341q. Epub 2008 Aug 12. J Am Chem Soc. 2008. PMID: 18693720
-
Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.Structure. 2009 Sep 9;17(9):1169-85. doi: 10.1016/j.str.2009.08.001. Structure. 2009. PMID: 19748338 Review.
Cited by
-
NMR Dynamic View of the Stabilization of the WW4 Domain by Neutral NaCl and Kosmotropic Na2SO4 and NaH2PO4.Int J Mol Sci. 2024 Aug 22;25(16):9091. doi: 10.3390/ijms25169091. Int J Mol Sci. 2024. PMID: 39201778 Free PMC article.
-
NMR Dynamic View of the Destabilization of WW4 Domain by Chaotropic GdmCl and NaSCN.Int J Mol Sci. 2024 Jul 4;25(13):7344. doi: 10.3390/ijms25137344. Int J Mol Sci. 2024. PMID: 39000450 Free PMC article.
-
A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain.Protein Sci. 2023 Jun;32(6):e4645. doi: 10.1002/pro.4645. Protein Sci. 2023. PMID: 37096906 Free PMC article. Review.
-
Protein Design: From the Aspect of Water Solubility and Stability.Chem Rev. 2022 Sep 28;122(18):14085-14179. doi: 10.1021/acs.chemrev.1c00757. Epub 2022 Aug 3. Chem Rev. 2022. PMID: 35921495 Free PMC article. Review.
-
Adenosine triphosphate energy-independently controls protein homeostasis with unique structure and diverse mechanisms.Protein Sci. 2021 Jul;30(7):1277-1293. doi: 10.1002/pro.4079. Epub 2021 Apr 13. Protein Sci. 2021. PMID: 33829608 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources