[NMR paper] The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
Most techniques allow detection of protein unfolding either by following the behaviour of single reporters or as an averaged all-or-none process. We recently added 2D NMR spectroscopy to the well-established techniques able to obtain information on the process of unfolding using resonances of residues in the hydrophobic core of a protein. Here, we questioned whether an analysis of the individual stability curves from each resonance could provide additional site-specific...
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03-05-2022 01:44 AM
Site-Specific Protein Internal Motions Revealed by 2H Solid-State NMR Spectroscopy
Site-Specific Protein Internal Motions Revealed by 2H Solid-State NMR Spectroscopy
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Xiangyan Shi, Deborah A. Berthold, Chad M. Rienstra</br>
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02-17-2016 07:50 PM
[NMR paper] Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D (2)H-(13)C-(13)C Solid-State NMR Spectroscopy.
Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D (2)H-(13)C-(13)C Solid-State NMR Spectroscopy.
Related Articles Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D (2)H-(13)C-(13)C Solid-State NMR Spectroscopy.
J Am Chem Soc. 2016 Feb 5;
Authors: Shi X, Rienstra CM
Abstract
(2)H quadrupolar line shapes deliver rich information about protein dynamics. A newly designed 3D (2)H-(13)C-(13)Csolid-state NMR magic angle spinning (MAS) experiment is presented and demonstrated on the...
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02-06-2016 03:10 PM
The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method
The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method
Abstract Protein internal motions influence observables of NMR experiments. The effect of internal motions occurring at the sub-nanosecond timescale can be described by NMR order parameters. Here, we report that the use of order parameters derived from Molecular Dynamics (MD) simulations of two holo-structures of Protein Kinase A increase the discrimination power of INPHARMA, an NMR based methodology that selects docked ligand orientations by maximizing the correlation of...
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09-24-2012 01:02 AM
[NMR paper] Characterization of the internal motions of a chimeric protein by 13C NMR highlights
Characterization of the internal motions of a chimeric protein by 13C NMR highlights the important dynamic consequences of the engineering on a millisecond time scale.
Related Articles Characterization of the internal motions of a chimeric protein by 13C NMR highlights the important dynamic consequences of the engineering on a millisecond time scale.
Eur J Biochem. 2000 Nov;267(22):6519-33
Authors: Wolff N, Guenneugues M, Gilquin B, Drakopoulou E, Vita C, Ménez A, Zinn-Justin S
By transferring the central curaremimetic beta hairpin of the...
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11-19-2010 08:29 PM
[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
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08-22-2010 03:31 PM
[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D - ACS Publications
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