Paramagnetic centers in biomolecules, such as specific metal ions that are bound to a protein, affect the nuclei in their surrounding in various ways. One of these effects is the pseudocontact shift (PCS), which leads to strong chemical shift perturbations of nuclear spins, with a remarkably long range of 50 Å and beyond. The PCS in solution NMR is an effect originating from the anisotropic part of the dipole-dipole interaction between the magnetic momentum of unpaired electrons and nuclear...
[NMR paper] NMR pseudocontact shifts in a symmetric protein homotrimer.
NMR pseudocontact shifts in a symmetric protein homotrimer.
Related Articles NMR pseudocontact shifts in a symmetric protein homotrimer.
J Biomol NMR. 2020 Jul 03;:
Authors: Müntener T, Böhm R, Atz K, Häussinger D, Hiller S
Abstract
NMR pseudocontact shifts are a valuable tool for structural and functional studies of proteins. Protein multimers mediate key functional roles in biology, but methods for their study by pseudocontact shifts are so far not available. Paramagnetic tags attached to identical subunits in multimeric...
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07-06-2020 10:08 AM
NMR pseudocontact shifts in a symmetric protein homotrimer
NMR pseudocontact shifts in a symmetric protein homotrimer
Abstract
NMR pseudocontact shifts are a valuable tool for structural and functional studies of proteins. Protein multimers mediate key functional roles in biology, but methods for their study by pseudocontact shifts are so far not available. Paramagnetic tags attached to identical subunits in multimeric proteins cause a combined pseudocontact shift that cannot be described by the standard single-point model. Here, we report pseudocontact shifts generated simultaneously by three paramagnetic...
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07-04-2020 03:45 AM
Methyl group assignment using pseudocontact shifts with PARAssign
Methyl group assignment using pseudocontact shifts with PARAssign
Abstract
A new version of the program PARAssign has been evaluated for assignment of NMR resonances of the 76 methyl groups in leucines, isoleucines and valines in a 25Â*kDa protein, using only the structure of the protein and pseudocontact shifts (PCS) generated with a lanthanoid tag at up to three attachment sites. The number of reliable assignments depends strongly on two factors. The principle axes of the magnetic susceptibility tensors of the paramagnetic centers should not be...
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11-27-2017 01:29 PM
[NMR paper] Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags.
Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags.
Related Articles Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags.
Prog Nucl Magn Reson Spectrosc. 2017 Feb;98-99:20-49
Authors: Nitsche C, Otting G
PMID: 28283085
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03-12-2017 12:32 PM
Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags
Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags
Publication date: Available online 1 December 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Christoph Nitsche, Gottfried Otting</br>
Graphical abstract
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12-02-2016 07:45 AM
Proteinâ??protein HADDocking using exclusively pseudocontact shifts
Proteinâ??protein HADDocking using exclusively pseudocontact shifts
<div class="Abstract" lang="en">Abstract <div class="normal">In order to enhance the structure determination process of macromolecular assemblies by NMR, we have implemented long-range pseudocontact shift (PCS) restraints into the data-driven protein docking package HADDOCK. We demonstrate the efficiency of the method on a synthetic, yet realistic case based on the lanthanide-labeled N-terminal ε domain of the E. coli DNA polymerase III (ε186) in complex with the HOT domain. Docking from the bound form of the two...
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06-06-2011 12:53 AM
Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded
Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)-Binding Amino Acid.
Related Articles Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)-Binding Amino Acid.
Angew Chem Int Ed Engl. 2010 Nov 25;
Authors: Nguyen TH, Ozawa K, Stanton-Cook M, Barrow R, Huber T, Otting G
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[NMR paper] Improving the accuracy of NMR structures of large proteins using pseudocontact shifts
Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.
Related Articles Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.
J Biomol NMR. 2004 Mar;28(3):205-12
Authors: Gaponenko V, Sarma SP, Altieri AS, Horita DA, Li J, Byrd RA
We demonstrate improved accuracy in protein structure determination for large (>/=30 kDa), deuterated proteins (e.g. STAT4(NT)) via the combination of pseudocontact shifts for amide and methyl protons...
Pseudocontact Shifts in Biomolecular NMR Spectroscopy
Linear Mode
