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 analysis of ^(19)F NMR-monitored...
[NMR paper] Comprehensive analysis of NMR data using advanced line shape fitting.
Comprehensive analysis of NMR data using advanced line shape fitting.
Related Articles Comprehensive analysis of NMR data using advanced line shape fitting.
J Biomol NMR. 2017 Oct 17;:
Authors: Niklasson M, Otten R, Ahlner A, Andresen C, Schlagnitweit J, Petzold K, Lundström P
Abstract
NMR spectroscopy is uniquely suited for atomic resolution studies of biomolecules such as proteins, nucleic acids and metabolites, since detailed information on structure and dynamics are encoded in positions and line shapes of peaks in NMR...
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10-19-2017 10:47 PM
Comprehensive analysis of NMR data using advanced line shape fitting
Comprehensive analysis of NMR data using advanced line shape fitting
Abstract
NMR spectroscopy is uniquely suited for atomic resolution studies of biomolecules such as proteins, nucleic acids and metabolites, since detailed information on structure and dynamics are encoded in positions and line shapes of peaks in NMR spectra. Unfortunately, accurate determination of these parameters is often complicated and time consuming, in part due to the need for different software at the various analysis steps and for validating the results. Here, we present an...
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10-17-2017 10:19 AM
[NMR paper] NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase.
NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase.
Related Articles NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase.
J Biomol NMR. 2017 Apr 09;:
Authors: Shinya S, Ghinet MG, Brzezinski R, Furuita K, Kojima C, Shah S, Kovrigin EL, Fukamizo T
Abstract
Chitosan interaction with chitosanase was examined through analysis of spectral line shapes in the NMR HSQC titration experiments. We established that the substrate, chitosan hexamer, binds to the enzyme through the...
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04-11-2017 04:27 PM
NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase
NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase
Abstract
Chitosan interaction with chitosanase was examined through analysis of spectral line shapes in the NMR HSQC titration experiments. We established that the substrate, chitosan hexamer, binds to the enzyme through the three-state induced-fit mechanism with fast formation of the encounter complex followed by slow isomerization of the bound-state into the final conformation. Mapping of the chemical shift perturbations in two sequential steps of the mechanism...
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04-10-2017 12:51 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] Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain fold
Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
Related Articles Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
J Am Chem Soc. 2003 May 21;125(20):6032-3
Authors: Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP
There is considerable interest in small proteins that fold very rapidly. These proteins have become attractive targets for both theoretical and computational studies. The...
Line Shape Analysis of 19F NMR-Monitored Chemical Denaturation of a Fold-Switching Protein RfaH Reveals Its Slow Folding Dynamics
Linear Mode
