[NMR paper] Line Shape Analysis of 19F NMR-Monitored Chemical Denaturation of a Fold-Switching Protein RfaH Reveals Its Slow Folding Dynamics
Line Shape Analysis of 19F NMR-Monitored Chemical Denaturation of a Fold-Switching Protein RfaH Reveals Its Slow Folding Dynamics
The recent discovery of metamorphic proteins, which can switch between multiple conformations under native conditions, has challenged the well-established one sequence-one structure paradigm of protein folding. This is exemplified in the C-terminal domain of the multidomain transcription factor RfaH, which converts from an ?-helical coiled-coil conformation in its autoinhibited state to a ?-barrel conformation upon activation. Here, we use multisite line shape...
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11-22-2023 06:46 PM
[ASAP] Folding of Circularly Permuted and Split Outer Membrane Protein F via Electrostatic Interactions with Terminal Residues
Folding of Circularly Permuted and Split Outer Membrane Protein F via Electrostatic Interactions with Terminal Residues
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00195/20210601/images/medium/bi1c00195_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00195
http://feeds.feedburner.com/~r/acs/bichaw/~4/8DFN1W6q71s
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06-01-2021 11:42 PM
Electron microscopes close to imaging individual atoms - Science /AAAS
http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcQ7W5DfRyKowTkltGG0zjTrIKEAzUZDTdGE2Cc29ak827pQR_FXlISI-IMAFeQljXSf6uDzWlNe
Science /AAAS
<img alt="" height="1" width="1">
Electron microscopes close to imaging individual atoms
Science /AAAS
The two main power tools, x-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, enable researchers to pin down the position of protein features to less than 0.2 nanometers, good enough to see individual atoms. By contrast, cryo-EM ...
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Electron microscopes close to imaging individual atoms - Science...
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05-08-2015 09:14 AM
[NMR paper] Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
Related Articles Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
J Mol Biol. 2014 Feb 11;
Authors: Kukic P, Camilloni C, Cavalli A, Vendruscolo M
Abstract
Many protein molecules are formed by two or more domains whose structures and dynamics are closely related to their biological functions. It is thus important to develop methods to...
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02-19-2014 12:07 AM
[NMR paper] Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
J Phys Chem B. 2013 Jun 24;
Authors: Campos LA, Sadqi M, Liu J, Wang X, English DS, Munoz V
Abstract
Theory predicts that folding free energy landscapes are intrinsically malleable, and as such are expected to respond to perturbations in topographically complex...
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06-27-2013 01:52 AM
[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
J Mol Biol. 2003 May 16;328(5):1161-71
Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ
At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...
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11-24-2010 09:01 PM
[NMR paper] Protein folding monitored at individual residues during a two-dimensional NMR experim
Protein folding monitored at individual residues during a two-dimensional NMR experiment.
Related Articles Protein folding monitored at individual residues during a two-dimensional NMR experiment.
Science. 1996 Nov 15;274(5290):1161-3
Authors: Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM
An approach is described to monitor directly at the level of individual residues the formation of structure during protein folding. A two-dimensional heteronuclear nuclear magnetic resonance (NMR) spectrum was recorded after the rapid...
Protein Folding Monitored at Individual Residues During a Two-Dimensional NMR Experiment - Science
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