Longitudinal relaxation properties of (1)H(N) and (1)H(α) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs)

Journal of Magnetic Resonance
Tomáš HošekIsabella C Felli

Abstract

Intrinsically disordered proteins (IDPs) are functional proteins containing large fragments characterized by high local mobility. Bioinformatic studies have suggested that a significant fraction (more than 30%) of eukaryotic proteins has disordered regions of more than 50 amino acids in length. Hence, NMR methods for the characterization of local compactness and solvent accessibility in such highly disordered proteins are of high importance. Among the available approaches, the HET-SOFAST/BEST experiments (Schanda et al., 2006, Rennella et al., 2014) provide semi-quantitative information by monitoring longitudinal (1)H relaxation of amide protons under different initial conditions. However, when approaching physiological sample conditions, the potential of these amide (1)H detected experiments is reduced due to rapid amide proton solvent exchange. (13)C direct detection methods therefore provide a valuable alternative thanks to a higher chemical shift dispersion and their intrinsic insensitivity toward solvent exchange. Here we present two sets of (13)C-detected experiments, which indirectly measure (1)H(N) and (1)H(α) inversion recovery profiles. The experiments consist of an initial spin inversion-recovery block optimized for ...Continue Reading

References

May 31, 2001·Journal of Molecular Graphics & Modelling·A K DunkerZ Obradovic
May 23, 2002·Biochemistry·A Keith DunkerZoran Obradović
Oct 24, 2002·Journal of the American Chemical Society·Konstantin PervushinAlexander Eletsky
Jun 2, 2005·Journal of the American Chemical Society·Paul Schanda, Bernhard Brutscher
Jun 2, 2005·Journal of Biomolecular NMR·Donghan LeeKonstantin Pervushin
Jun 9, 2005·Protein Expression and Purification·Chunjuan HuangChih-chen Wang
Oct 13, 2005·The FEBS Journal·A Keith DunkerVladimir N Uversky
Oct 27, 2005·Journal of Magnetic Resonance·Michaël Deschamps, Iain D Campbell
Mar 23, 2006·Journal of the American Chemical Society·Wolfgang BermelRoberta Pierattelli
Jun 23, 2006·Journal of Biomolecular NMR·Francesco FioritoKurt Wüthrich
Jul 11, 2006·Magnetic Resonance in Chemistry : MRC·Paul SchandaBernhard Brutscher
Dec 7, 2007·Trends in Biochemical Sciences·Peter Tompa, Monika Fuxreiter
Dec 26, 2007·Journal of Magnetic Resonance·Giuseppe Pileio, Malcolm H Levitt
Jan 23, 2009·Current Opinion in Structural Biology·Peter E Wright, H Jane Dyson
Feb 20, 2009·PLoS Biology·Marco D MukraschMarkus Zweckstetter
Mar 25, 2009·Journal of Magnetic Resonance·Wolfgang BermelPeter Tompa
May 23, 2009·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Isabella C Felli, Bernhard Brutscher
Oct 3, 2009·Journal of the American Chemical Society·Wolfgang BermelRoberta Pierattelli
May 4, 2010·Journal of Biomolecular NMR·Sampo MäntylahtiPerttu Permi
Aug 7, 2010·Journal of the American Chemical Society·Rhagavendran L NarayananMarkus Zweckstetter
Mar 23, 2011·Journal of Biomolecular NMR·Jiří NováčekVladimír Sklenář
Apr 26, 2011·Current Opinion in Structural Biology·Peter Tompa
Jun 12, 2012·Journal of Biomolecular NMR·Wolfgang BermelJan Stanek
Jul 19, 2012·Magnetic Resonance in Chemistry : MRC·Swagata ChakrabortyRamakrishna V Hosur
Feb 26, 2013·Journal of Biomolecular NMR·Zsofia SolyomBernhard Brutscher
Jun 25, 2013·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Krzysztof KazimierczukWiktor Koźmiński
Jun 25, 2013·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Jaka KrageljMalene Ringkjøbing Jensen
Nov 10, 2013·Journal of Biomolecular NMR·Wolfgang BermelAnna Zawadzka-Kazimierczuk
Mar 25, 2014·Journal of Magnetic Resonance·Jiří NováčekVladimír Sklenář
Mar 25, 2014·Journal of Magnetic Resonance·Robert Konrat

❮ Previous
Next ❯

Citations

Feb 2, 2016·Journal of Magnetic Resonance·G ChalmersJ H Prestegard
May 16, 2017·Archives of Biochemistry and Biophysics·Eric B GibbsScott A Showalter
Jan 21, 2021·Magnetic Resonance in Chemistry : MRC·Lianne H E Wieske, Máté Erdélyi
Mar 13, 2018·Analytical Chemistry·Or SzekelyLucio Frydman

❮ Previous
Next ❯

Related Concepts

Related Feeds

Alpha-Synuclein Aggregation (MDS)

Alpha-synucleins are small proteins that are believed to restrict the mobility of synpatic vesicles and inhibit neurotransmitter release. Aggregation of these proteins have been linked to several types of neurodegenerative diseases including dementia with Lewy bodies and Parkinson's disease. Here is the latest research on α-synuclein aggregation.