Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts.

Biochemistry
Carlo CamilloniMichele Vendruscolo

Abstract

One of the major open challenges in structural biology is to achieve effective descriptions of disordered states of proteins. This problem is difficult because these states are conformationally highly heterogeneous and cannot be represented as single structures, and therefore it is necessary to characterize their conformational properties in terms of probability distributions. Here we show that it is possible to obtain highly quantitative information about particularly important types of probability distributions, the populations of secondary structure elements (α-helix, β-strand, random coil, and polyproline II), by using the information provided by backbone chemical shifts. The application of this approach to mammalian prions indicates that for these proteins a key role in molecular recognition is played by disordered regions characterized by highly conserved polyproline II populations. We also determine the secondary structure populations of a range of other disordered proteins that are medically relevant, including p53, α-synuclein, and the Aβ peptide, as well as an oligomeric form of αB-crystallin. Because chemical shifts are the nuclear magnetic resonance parameters that can be measured under the widest variety of conditi...Continue Reading

References

Nov 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·J Horwitz
Jan 1, 1994·Methods in Enzymology·D S Wishart, B D Sykes
Aug 28, 1997·Nature·M G SpillantiniM Goedert
Nov 13, 1998·Proceedings of the National Academy of Sciences of the United States of America·S B Prusiner
Mar 26, 1999·Protein Science : a Publication of the Protein Society·B J Stapley, T P Creamer
Jan 5, 2000·Proceedings of the National Academy of Sciences of the United States of America·R ZahnK Wüthrich
Jul 18, 2001·Journal of the American Chemical Society·S SchwarzingerH J Dyson
Mar 23, 2002·Protein Science : a Publication of the Protein Society·Yunjun Wang, Oleg Jardetzky
Jan 23, 2003·Protein Science : a Publication of the Protein Society·Ling-Hong Hung, Ram Samudrala
Feb 15, 2003·The Journal of Biological Chemistry·Sreeganga ChandraThomas C Südhof
Dec 19, 2003·Nucleic Acids Research·Michael Y Galperin
Dec 20, 2003·Nature·Christopher M Dobson
Jun 25, 2004·Nucleic Acids Research·Matthias Heinig, Dmitrij Frishman
Mar 2, 2005·Nature Reviews. Molecular Cell Biology·H Jane Dyson, Peter E Wright
Dec 24, 2005·Proceedings of the National Academy of Sciences of the United States of America·Joerg GsponerMichele Vendruscolo
May 11, 2006·Chemical Reviews·Zhengshuang ShiNeville R Kallenbach
Nov 1, 2006·Protein and Peptide Letters·Rita BerisioLuigi Vitagliano
Nov 8, 2006·Protein Science : a Publication of the Protein Society·Joseph A MarshJulie D Forman-Kay
Nov 24, 2006·Proceedings of the National Academy of Sciences of the United States of America·J U RevelesA W Castleman
Mar 24, 2007·Nature Reviews. Molecular Cell Biology·Karen H Vousden, David P Lane
Apr 18, 2007·Proceedings of the National Academy of Sciences of the United States of America·Daniel P TeufelAlan R Fersht
May 31, 2007·Proceedings of the National Academy of Sciences of the United States of America·Andrea CavalliMichele Vendruscolo
Mar 11, 2008·Proceedings of the National Academy of Sciences of the United States of America·Yang ShenAd Bax
Apr 9, 2008·Proceedings of the National Academy of Sciences of the United States of America·Mark WellsAlan R Fersht
May 9, 2008·Nucleic Acids Research·Christian ColeGeoffrey J Barton
Jun 3, 2008·Journal of Molecular Biology·Gian Gaetano TartagliaMichele Vendruscolo
Nov 5, 2008·Journal of the American Chemical Society·Rinaldo W MontalvaoMichele Vendruscolo
Nov 27, 2008·Journal of Biomolecular NMR·Yang ShenAd Bax
Dec 17, 2008·Structure·Paul RobustelliMichele Vendruscolo
Feb 28, 2009·Human Molecular Genetics·Natalia NinkinaVladimir L Buchman
May 2, 2009·Nucleic Acids Research·Mark BerjanskiiDavid S Wishart
Jun 2, 2009·Journal of Molecular Biology·Jampani Nageswara RaoTobias S Ulmer
Oct 27, 2009·Journal of the American Chemical Society·Alfonso De SimoneMichele Vendruscolo
Oct 30, 2009·Proceedings of the National Academy of Sciences of the United States of America·Rhiju DasDavid Baker
Dec 10, 2009·Protein Science : a Publication of the Protein Society·Yang ShenAd Bax
Dec 18, 2009·Journal of Magnetic Resonance·Ming-Sin CheungR William Broadhurst

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Citations

Jan 9, 2013·Journal of Biomolecular NMR·James H PrestegardChristian Gruta
Jul 4, 2012·Journal of the American Chemical Society·Vincent A VoelzVijay S Pande
Aug 21, 2012·Journal of the American Chemical Society·Valéry OzenneMartin Blackledge
Jun 27, 2013·Proceedings of the National Academy of Sciences of the United States of America·David S LibichG Marius Clore
Nov 20, 2013·Proceedings of the National Academy of Sciences of the United States of America·Alessandro BarducciMichele Parrinello
May 14, 2014·Proceedings of the National Academy of Sciences of the United States of America·Alexander J F EganJean-Pierre Simorre
Jul 4, 2013·Biomolecular NMR Assignments·Shu-Ju Micky HsiehShang-Te Danny Hsu
Jul 9, 2013·Biomolecular NMR Assignments·Shang-Te Danny Hsu
Jul 16, 2014·Proceedings of the National Academy of Sciences of the United States of America·Geneviève DesjardinsLawrence P McIntosh
Dec 3, 2014·Progress in Nuclear Magnetic Resonance Spectroscopy·Wim F Vranken
Oct 3, 2014·Journal of Biomolecular NMR·Noor E Hafsa, David S Wishart
Feb 24, 2016·Journal of Magnetic Resonance·Arthur G Palmer
Feb 24, 2016·Frontiers in Molecular Biosciences·Jakob T Nielsen, Frans A A Mulder
Sep 24, 2014·Proceedings of the National Academy of Sciences of the United States of America·Peter M HwangBrian D Sykes
Feb 5, 2016·Biochimica Et Biophysica Acta·J Ignacio GalleaM Soledad Celej
Apr 3, 2013·Current Opinion in Structural Biology·Malene Ringkjøbing JensenMartin Blackledge
Nov 10, 2012·Advanced Drug Delivery Reviews·Lena Mäler
Feb 17, 2015·FEBS Open Bio·Scarlett SzpryngielLena Mäler
Sep 4, 2015·Protein Science : a Publication of the Protein Society·Maria K Janowska, Jean Baum
Mar 1, 2016·Chemical Reviews·Veronika CsizmokJulie D Forman-Kay
Oct 2, 2015·Biological & Pharmaceutical Bulletin·Maho Yagi-Utsumi, Christopher M Dobson
Nov 25, 2014·Biophysical Journal·Alfonso De Simone
Jun 25, 2013·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Jaka KrageljMalene Ringkjøbing Jensen
Jul 3, 2013·Chembiochem : a European Journal of Chemical Biology·Julien RocheAd Bax
May 9, 2012·Angewandte Chemie·Juan Miguel Lopez del AmoBernd Reif
Jan 21, 2014·Protein Science : a Publication of the Protein Society·Agnieszka A KendrickElan Z Eisenmesser
Aug 26, 2014·Protein Science : a Publication of the Protein Society·Hoi Tik Alvin LeungMichele Vendruscolo

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