scholarly journals P4T-DOTA – a lanthanide chelating tag combining a sterically highly overcrowded backbone with a reductively stable linker

2019 ◽  
Vol 55 (71) ◽  
pp. 10543-10546 ◽  
Author(s):  
Daniel Joss ◽  
Daniel Häussinger
Keyword(s):  
Structural Analysis ◽  
Residual Dipolar Couplings ◽  
Lanthanide Complex ◽  
Dipolar Couplings ◽  
Pseudocontact Shifts

A highly rigidified lanthanide complex induces strong pseudocontact shifts and residual dipolar couplings for structural analysis of proteins in solution.

Paramagpy: Software for Fitting Magnetic Susceptibility Tensors Using Paramagnetic Effects Measured in NMR Spectra

2019 ◽  
Author(s):  
Henry Orton ◽  
Thomas Huber ◽  
Gottfried Otting
Keyword(s):  
Experimental Data ◽  
Magnetic Susceptibility ◽  
Nmr Spectra ◽  
Residual Dipolar Couplings ◽  
Paramagnetic Relaxation ◽  
Dipolar Couplings ◽  
Paramagnetic Susceptibility ◽  
Pseudocontact Shifts ◽  
Seamless Transition ◽  
Paramagnetic Relaxation Enhancements

Paramagpy is a python module for calculating paramagnetic effects in NMR spectra of proteins. This currently includes fitting of paramagnetic susceptibility tensors to experimental data associated with pseudocontact shifts (PCS) residual dipolar couplings (RDC), paramagnetic relaxation enhancements (PRE) and cross-correlated relaxation (CCR). A GUI allows easy viewing of data and seamless transition between PCS/RDC/PRE/CCR calculations.<br><br>

Paramagpy: Software for Fitting Magnetic Susceptibility Tensors Using Paramagnetic Effects Measured in NMR Spectra

2019 ◽  
Author(s):  
Henry Orton ◽  
Thomas Huber ◽  
Gottfried Otting
Keyword(s):  
Experimental Data ◽  
Magnetic Susceptibility ◽  
Nmr Spectra ◽  
Residual Dipolar Couplings ◽  
Paramagnetic Relaxation ◽  
Dipolar Couplings ◽  
Paramagnetic Susceptibility ◽  
Pseudocontact Shifts ◽  
Seamless Transition ◽  
Paramagnetic Relaxation Enhancements

Paramagpy is a python module for calculating paramagnetic effects in NMR spectra of proteins. This currently includes fitting of paramagnetic susceptibility tensors to experimental data associated with pseudocontact shifts (PCS) residual dipolar couplings (RDC), paramagnetic relaxation enhancements (PRE) and cross-correlated relaxation (CCR). A GUI allows easy viewing of data and seamless transition between PCS/RDC/PRE/CCR calculations.<br><br>

scholarly journals Simultaneous use of solution NMR and X-ray data inREFMAC5 for joint refinement/detection of structural differences

2014 ◽  
Vol 70 (4) ◽  
pp. 958-967 ◽  
Author(s):  
Mauro Rinaldelli ◽  
Enrico Ravera ◽  
Vito Calderone ◽  
Giacomo Parigi ◽  
Garib N. Murshudov ◽  
...  
Keyword(s):  
Solid State ◽  
Residual Dipolar Couplings ◽  
Catalytic Domain ◽  
Dipolar Couplings ◽  
Crystallographic Data ◽  
Paramagnetic Nmr ◽  
Pseudocontact Shifts ◽  
X Ray ◽  
Matrix Metalloproteinase 1 ◽  
Simultaneous Use

The programREFMAC5 fromCCP4 was modified to allow the simultaneous use of X-ray crystallographic data and paramagnetic NMR data (pseudocontact shifts and self-orientation residual dipolar couplings) and/or diamagnetic residual dipolar couplings. Incorporation of these long-range NMR restraints inREFMAC5 can reveal differences between solid-state and solution conformations of molecules or, in their absence, can be used together with X-ray crystallographic data for structural refinement. Since NMR and X-ray data are complementary, when a single structure is consistent with both sets of data and still maintains reasonably `ideal' geometries, the reliability of the derived atomic model is expected to increase. The program was tested on five different proteins: the catalytic domain of matrix metalloproteinase 1, GB3, ubiquitin, free calmodulin and calmodulin complexed with a peptide. In some cases the joint refinement produced a single model consistent with both sets of observations, while in other cases it indicated, outside the experimental uncertainty, the presence of different protein conformations in solution and in the solid state.

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