Wenguang HeGenevičve M. C. Gasmi-SeabrookMitsuhiko IkuraJeffrey E. LeeMichael OhhaDepartment of Biochemistry, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5G 1M1, CanadabPrincess Margaret Cancer Centre, University Health Network, Toronto, ON M5G 1L7, CanadacDepartment of Medical Biophysics, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5G 1L7, CanadadDepartment of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, Canada...
Date:
Proceedings of the National Academy of Sciences, Volume 121, Issue 37, September 2024. Read More
[NMR paper] Translational Diffusion and Self-Association of an Intrinsically Disordered Protein kappa-Casein Using NMR with Ultra-High Pulsed-Field Gradient and Time-Resolved FRET
Translational Diffusion and Self-Association of an Intrinsically Disordered Protein kappa-Casein Using NMR with Ultra-High Pulsed-Field Gradient and Time-Resolved FRET
Much attention has been given to studying the translational diffusion of globular proteins, whereas the translational diffusion of intrinsically disordered proteins (IDPs) is less studied. In this study, we investigate the translational diffusion and how it is affected by the self-association of an IDP, ?-casein, using pulsed-field gradient nuclear magnetic resonance and time-resolved Förster resonance energy transfer. Using...
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[NMR paper] Influence of an Intrinsically Disordered Region on Protein Domains Revealed by NMR-Based Electrostatic Potential Measurements
Influence of an Intrinsically Disordered Region on Protein Domains Revealed by NMR-Based Electrostatic Potential Measurements
Many human proteins possess intrinsically disordered regions containing consecutive aspartate or glutamate residues ("D/E repeats"). Approximately half of them are DNA/RNA-binding proteins. In this study, using nuclear magnetic resonance (NMR) spectroscopy, we investigated the electrostatic properties of D/E repeats and their influence on folded domains within the same protein. Local electrostatic potentials were directly measured for the HMGB1 protein, its isolated...
[NMR paper] Surface Accessibility of an Intrinsically Disordered Protein Probed by 2D Time-Resolved Laser-Assisted NMR Spectroscopy
Surface Accessibility of an Intrinsically Disordered Protein Probed by 2D Time-Resolved Laser-Assisted NMR Spectroscopy
Probing the protein surface accessibility of different residues is a powerful way of characterizing the overall conformation of intrinsically disordered proteins (IDPs). We present a two-dimensional (2D) time-resolved photo-CIDNP (TR-CIDNP) experiment suitable for IDP analysis. Pulse stretching of high-power laser pulses, band-selective decoupling of ^(13)C^(?), and simultaneous application of radiofrequency and laser pulses were implemented to quantitatively analyze the...
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[NMR paper] Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
Related Articles Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
J Am Chem Soc. 2017 Aug 07;:
Authors: Charlier C, Bouvignies G, Pelupessy P, Walrant A, Marquant R, Kozlov M, De Ioannes P, Bolik-Coulon N, Sagan S, Cortes P, Aggarwal AK, Carlier L, Ferrage F
Abstract
Many intrinsically disordered proteins (IDPs) and protein...
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[NMR paper] Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy.
Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy.
Related Articles Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy.
Biochim Biophys Acta. 2016 Jun 8;
Authors: Yao S, Lee EF, Pettikiriarachchi A, Evangelista M, Keizer DW, Fairlie WD
Abstract
Beclin 1 is a 450 amino acid protein that plays critical roles in the early stages of autophagosome...
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[NMR paper] Novel methods based on 13C detection to study intrinsically disordered proteins
Novel methods based on 13C detection to study intrinsically disordered proteins
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Isabella C. Felli , Roberta Pierattelli</br>
Intrinsically disordered proteins (IDPs) are characterized by highly flexible solvent exposed backbones and can sample many different conformations. These properties confer them functional advantages, complementary to those of folded proteins, which need to be characterized to expand our view of how protein structural and dynamic features affect...
Time-resolved NMR detection of prolyl-hydroxylation in intrinsically disordered region of HIF-1?
Linear Mode
