[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...
[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...
F NMR-Monitored Chemical Denaturation of a Fold-Switching Protein RfaH Reveals Its Slow Folding Dynamics - ACS Publications
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