Understanding disordered and unfolded proteins using single-molecule FRET and polymer theory
- PMID: 28192291
- DOI: 10.1088/2050-6120/4/4/042003
Understanding disordered and unfolded proteins using single-molecule FRET and polymer theory
Abstract
Understanding protein folding and the functional properties of intrinsically disordered proteins (IDPs) requires detailed knowledge of the forces that act in polypeptide chains. These forces determine the dimensions and dynamics of unfolded and disordered proteins and have been suggested to impact processes such as the coupled binding and folding of IDPs, or the rate of protein folding reactions. Much of the progress in understanding the physical and chemical properties of unfolded and intrinsically disordered polypeptide chains has been made possible by the recent developments in single-molecule fluorescence techniques. However, the interpretation of the experimental results requires concepts from polymer physics in order to be understood. Here, I review some of the theories used to describe the dimensions of unfolded polypeptide chains under varying solvent conditions together with their more recent application to experimental data.
Similar articles
-
Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins.Annu Rev Biophys. 2016 Jul 5;45:207-31. doi: 10.1146/annurev-biophys-062215-010915. Epub 2016 May 2. Annu Rev Biophys. 2016. PMID: 27145874 Review.
-
Perspective: Chain dynamics of unfolded and intrinsically disordered proteins from nanosecond fluorescence correlation spectroscopy combined with single-molecule FRET.J Chem Phys. 2018 Jul 7;149(1):010901. doi: 10.1063/1.5037683. J Chem Phys. 2018. PMID: 29981536
-
Single-molecule spectroscopy of unfolded proteins and chaperonin action.Biol Chem. 2014 Jul;395(7-8):689-98. doi: 10.1515/hsz-2014-0132. Biol Chem. 2014. PMID: 24620016 Review.
-
Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations.Proc Natl Acad Sci U S A. 2017 Mar 7;114(10):E1833-E1839. doi: 10.1073/pnas.1616672114. Epub 2017 Feb 21. Proc Natl Acad Sci U S A. 2017. PMID: 28223518 Free PMC article.
-
Polymer effects modulate binding affinities in disordered proteins.Proc Natl Acad Sci U S A. 2019 Sep 24;116(39):19506-19512. doi: 10.1073/pnas.1904997116. Epub 2019 Sep 5. Proc Natl Acad Sci U S A. 2019. PMID: 31488718 Free PMC article.
Cited by
-
Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology.Biomolecules. 2023 Jan 7;13(1):124. doi: 10.3390/biom13010124. Biomolecules. 2023. PMID: 36671509 Free PMC article. Review.
-
Hypothesis: structural heterogeneity of the unfolded proteins originating from the coupling of the local clusters and the long-range distance distribution.Biophys Rev. 2018 Apr;10(2):363-373. doi: 10.1007/s12551-018-0405-8. Epub 2018 Feb 14. Biophys Rev. 2018. PMID: 29446056 Free PMC article. Review.
-
Protein unfolding mechanisms and their effects on folding experiments.F1000Res. 2017 Sep 22;6:1723. doi: 10.12688/f1000research.12070.1. eCollection 2017. F1000Res. 2017. PMID: 29034084 Free PMC article. Review.
-
Single-Molecule FRET of Membrane Transport Proteins.Chembiochem. 2021 Sep 2;22(17):2657-2671. doi: 10.1002/cbic.202100106. Epub 2021 May 21. Chembiochem. 2021. PMID: 33945656 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
