The role of protein-solvent interactions in protein unfolding
- PMID: 8768902
- DOI: 10.1016/s0958-1669(96)80119-4
The role of protein-solvent interactions in protein unfolding
Abstract
Protein unfolding occurs when the balance of forces between the protein's interaction with itself and the protein's interaction with its environment is disrupted. The disruption of this balance of forces may be as simple as a perturbance of the normal water structure around the protein. A decrease in the normal water-water interaction will result in an increase in the relative interaction of water with the protein. An increase in the number of interactions between water and the protein may initiate a protein's unfolding. This model for protein unfolding is supported by a range of recent experimental and computational data.
Similar articles
-
The molecular basis for the chemical denaturation of proteins by urea.Proc Natl Acad Sci U S A. 2003 Apr 29;100(9):5142-7. doi: 10.1073/pnas.0930122100. Epub 2003 Apr 17. Proc Natl Acad Sci U S A. 2003. PMID: 12702764 Free PMC article.
-
Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding.Proc Natl Acad Sci U S A. 2008 Nov 4;105(44):16928-33. doi: 10.1073/pnas.0808427105. Epub 2008 Oct 28. Proc Natl Acad Sci U S A. 2008. PMID: 18957546 Free PMC article.
-
Competitive model on denaturant-mediated protein unfolding.Biophys J. 2003 Feb;84(2 Pt 1):770-4. doi: 10.1016/S0006-3495(03)74896-6. Biophys J. 2003. PMID: 12547761 Free PMC article.
-
Protein unfolding--an important process in vivo?Curr Opin Struct Biol. 2003 Feb;13(1):98-109. doi: 10.1016/s0959-440x(03)00010-1. Curr Opin Struct Biol. 2003. PMID: 12581666 Review.
-
Mechanisms of protein assembly: lessons from minimalist models.Acc Chem Res. 2006 Feb;39(2):135-42. doi: 10.1021/ar040204a. Acc Chem Res. 2006. PMID: 16489733 Review.
Cited by
-
A novel solid-phase site-specific PEGylation enhances the in vitro and in vivo biostabilty of recombinant human keratinocyte growth factor 1.PLoS One. 2012;7(5):e36423. doi: 10.1371/journal.pone.0036423. Epub 2012 May 4. PLoS One. 2012. PMID: 22574160 Free PMC article.
-
Native and nonnative conformational preferences in the urea-unfolded state of barstar.Protein Sci. 2004 Dec;13(12):3085-91. doi: 10.1110/ps.04805204. Epub 2004 Nov 10. Protein Sci. 2004. PMID: 15537753 Free PMC article.
-
Role of α-helical structure in organic solvent-activated homodimer of elastase strain K.Int J Mol Sci. 2011;12(9):5797-814. doi: 10.3390/ijms12095797. Epub 2011 Sep 9. Int J Mol Sci. 2011. PMID: 22016627 Free PMC article.
-
Changes in water structure induced by the guanidinium cation and implications for protein denaturation.J Phys Chem A. 2008 Oct 30;112(43):10939-48. doi: 10.1021/jp8058239. Epub 2008 Oct 8. J Phys Chem A. 2008. PMID: 18839935 Free PMC article.
-
Electrospray ionization-mass spectrometry and tandem mass spectrometry reveal self-association and metal-ion binding of hydrophobic peptides: a study of the gramicidin dimer.Biophys J. 2004 Jan;86(1 Pt 1):473-9. doi: 10.1016/S0006-3495(04)74125-9. Biophys J. 2004. PMID: 14695291 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources