[NMR paper] Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy
Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy
How proteins switch between various ligand-free and ligand-bound structures has been a key biophysical question ever since the postulation of the Monod-Wyman-Changeux and Koshland-Nemethy-Filmer models over six decades ago. The ability of NMR spectroscopy to provide structural and kinetic information on biomolecular conformational exchange places it in a unique position as an analytical tool to interrogate the mechanisms of biological processes such as protein folding and biomolecular complex...
...
nmrlearner
Journal club
0
05-26-2022 08:36 AM
[NMR paper] Determining Binding Kinetics of Intrinsically Disordered Proteins by NMR Spectroscopy.
Determining Binding Kinetics of Intrinsically Disordered Proteins by NMR Spectroscopy.
Related Articles Determining Binding Kinetics of Intrinsically Disordered Proteins by NMR Spectroscopy.
Methods Mol Biol. 2020;2141:663-681
Authors: Yang K, Arai M, Wright PE
Abstract
The unique structural flexibility of intrinsically disordered proteins (IDPs) is central to their diverse functions in cellular processes. Protein-protein interactions involving IDPs are frequently transient and dynamic in nature. Nuclear magnetic resonance...
nmrlearner
Journal club
0
07-23-2020 11:23 PM
[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...
nmrlearner
Journal club
0
08-07-2017 07:31 PM
[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...
Elucidating binding mechanisms and dynamics of intrinsically disordered protein complexes using NMR spectroscopy - ScienceDirect
Linear Mode
