Disordered proteins studied by chemical shifts
Disordered proteins studied by chemical shifts
January 2012
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 60</br>
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12-01-2012 06:10 PM
Disordered proteins studied by chemical shifts
Disordered proteins studied by chemical shifts
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 60</br>
Magnus Kjaergaard, Flemming M. Poulsen</br>
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03-09-2012 09:16 AM
Disordered proteins studied by chemical shifts
Disordered proteins studied by chemical shifts
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, Available online 12 October 2011</br>
Magnus*Kjaergaard, Flemming M.*Poulsen</br>
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10-14-2011 07:16 AM
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains
Abstract Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramagnetism-based restraints. These restraints were measured after inclusion of a lanthanide binding tag in the C-terminal domain to supplement the data obtained...
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08-13-2011 02:47 AM
Proteins Reveal Their Secrets Under Pressure - Chemical & Engineering News
Proteins Reveal Their Secrets Under Pressure - Chemical & Engineering News
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Proteins Reveal Their Secrets Under Pressure
Chemical & Engineering News
With the device, the researchers attempted an NMR experiment they call pressure perturbation transient state spectroscopy. The experiment begins with a pressure spike that unfolds a protein in solution in an NMR sample tube; then the protein refolds ...
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08-02-2011 12:25 AM
[NMR paper] Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its us
Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements.
Related Articles Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements.
J Biomol NMR. 2005 May;32(1):71-81
Authors: Eghbalnia HR, Wang L, Bahrami A, Assadi A, Markley JL
We present an energy model that combines information from the amino acid sequence of a protein and available NMR chemical shifts for the purposes of identifying low...
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11-25-2010 08:21 PM
[NMR paper] Residue-specific millisecond to microsecond fluctuations in bacteriorhodopsin induced
Residue-specific millisecond to microsecond fluctuations in bacteriorhodopsin induced by disrupted or disorganized two-dimensional crystalline lattice, through modified lipid-helix and helix-helix interactions, as revealed by 13C NMR.
Related Articles Residue-specific millisecond to microsecond fluctuations in bacteriorhodopsin induced by disrupted or disorganized two-dimensional crystalline lattice, through modified lipid-helix and helix-helix interactions, as revealed by 13C NMR.
Biochim Biophys Acta. 2002 Sep 20;1565(1):97-106
Authors: Saitô H,...
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11-24-2010 08:58 PM
[NMR paper] NMR chemical shifts and structure refinement in proteins.
NMR chemical shifts and structure refinement in proteins.
Related Articles NMR chemical shifts and structure refinement in proteins.
J Biomol NMR. 1993 Sep;3(5):607-12
Authors: Laws DD, de Dios AC, Oldfield E
Computation of the 13C alpha chemical shifts (or shieldings) of glycine, alanine and valine residues in bovine and Drosophila calmodulins and Staphylococcal nuclease, and comparison with experimental values, is reported using a gauge-including atomic orbital quantum-chemical approach. The full approximately 24 ppm shielding range is...