To fold or expand--a charged question
- PMID: 20682745
- PMCID: PMC2930424
- DOI: 10.1073/pnas.1008673107
To fold or expand--a charged question
Conflict of interest statement
The authors declare no conflict of interest.
Figures
Comment on
-
From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.Proc Natl Acad Sci U S A. 2010 Aug 17;107(33):14609-14. doi: 10.1073/pnas.1001743107. Epub 2010 Jul 16. Proc Natl Acad Sci U S A. 2010. PMID: 20639465 Free PMC article.
Similar articles
-
From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.Proc Natl Acad Sci U S A. 2010 Aug 17;107(33):14609-14. doi: 10.1073/pnas.1001743107. Epub 2010 Jul 16. Proc Natl Acad Sci U S A. 2010. PMID: 20639465 Free PMC article.
-
Single-molecule measurement of protein folding kinetics.Science. 2003 Aug 29;301(5637):1233-5. doi: 10.1126/science.1085399. Science. 2003. PMID: 12947198
-
Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold.J Biol Chem. 2009 Nov 27;284(48):33217-23. doi: 10.1074/jbc.M109.041624. Epub 2009 Oct 2. J Biol Chem. 2009. PMID: 19801540 Free PMC article.
-
Single-molecule folding.Curr Opin Struct Biol. 2003 Feb;13(1):88-97. doi: 10.1016/s0959-440x(03)00011-3. Curr Opin Struct Biol. 2003. PMID: 12581665 Review.
-
The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements.Chemphyschem. 2005 May;6(5):858-70. doi: 10.1002/cphc.200400617. Chemphyschem. 2005. PMID: 15884068 Review.
Cited by
-
Dynamics of the Tec-family tyrosine kinase SH3 domains.Protein Sci. 2016 Apr;25(4):852-64. doi: 10.1002/pro.2887. Epub 2016 Mar 18. Protein Sci. 2016. PMID: 26808198 Free PMC article.
-
Importance of electrostatic interactions in the association of intrinsically disordered histone chaperone Chz1 and histone H2A.Z-H2B.PLoS Comput Biol. 2012;8(7):e1002608. doi: 10.1371/journal.pcbi.1002608. Epub 2012 Jul 12. PLoS Comput Biol. 2012. PMID: 22807669 Free PMC article.
-
Position-, disorder-, and salt-dependent diffusion in binding-coupled-folding of intrinsically disordered proteins.Phys Chem Chem Phys. 2019 Mar 6;21(10):5634-5645. doi: 10.1039/c8cp06803h. Phys Chem Chem Phys. 2019. PMID: 30793144 Free PMC article.
References
-
- Uversky VN, Oldfield CJ, Dunker AK. Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu Rev Biophys. 2008;37:215–246. - PubMed
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources