Publication date: Available online 1 December 2016 Source:Progress in Nuclear Magnetic Resonance Spectroscopy
Author(s): Christoph Nitsche, Gottfried Otting
[NMR paper] Enantiomeric two-armed lanthanide-binding tags for complementary effects in paramagnetic NMR spectroscopy.
Enantiomeric two-armed lanthanide-binding tags for complementary effects in paramagnetic NMR spectroscopy.
Related Articles Enantiomeric two-armed lanthanide-binding tags for complementary effects in paramagnetic NMR spectroscopy.
Chem Commun (Camb). 2016 Jun 2;
Authors: Lee MD, Dennis ML, Swarbrick JD, Graham B
Abstract
Two-armed lanthanide-binding tags induce significant, long-range paramagnetic effects in the NMR spectra of attached proteins. An enantiomeric pair of rigid, two-armed, cyclen-based tags are reported that...
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06-03-2016 04:52 PM
Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags
Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags
Abstract
Pseudocontact shifts (PCS) induced by tags loaded with paramagnetic lanthanide ions provide powerful long-range structure information, provided the location of the metal ion relative to the target protein is known. Usually, the metal position is determined by fitting the magnetic susceptibility anisotropy (Ī?Ļ?) tensor to the 3D structure of the protein in an 8-parameter fit, which requires a large set of PCSs to be reliable. In an alternative...
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11-23-2015 06:58 PM
Integral membrane protein structure determination using pseudocontact shifts
Integral membrane protein structure determination using pseudocontact shifts
Abstract
Obtaining enough experimental restraints can be a limiting factor in the NMR structure determination of larger proteins. This is particularly the case for large assemblies such as membrane proteins that have been solubilized in a membrane-mimicking environment. Whilst in such cases extensive deuteration strategies are regularly utilised with the aim to improve the spectral quality, these schemes often limit the number of NOEs obtainable, making complementary...
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01-21-2015 08:39 PM
[NMR paper] Erratum to: PARAssign-paramagnetic NMR assignments of protein nuclei on the basis of pseudocontact shifts.
Erratum to: PARAssign-paramagnetic NMR assignments of protein nuclei on the basis of pseudocontact shifts.
Related Articles Erratum to: PARAssign-paramagnetic NMR assignments of protein nuclei on the basis of pseudocontact shifts.
J Biomol NMR. 2013 Jun 23;
Authors: Skinner SP, Moshev M, Hass MA, Keizers PH, Ubbink M
Abstract
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06-26-2013 09:39 AM
[NMR paper] PARAssign-paramagnetic NMR assignments of protein nuclei on the basis of pseudocontact shifts.
PARAssign-paramagnetic NMR assignments of protein nuclei on the basis of pseudocontact shifts.
Related Articles PARAssign-paramagnetic NMR assignments of protein nuclei on the basis of pseudocontact shifts.
J Biomol NMR. 2013 Mar 23;
Authors: Skinner SP, Moshev M, Hass MA, Ubbink M
Abstract
The use of paramagnetic NMR data for the refinement of structures of proteins and protein complexes is widespread. However, the power of paramagnetism for protein assignment has not yet been fully exploited. PARAssign is software that uses...
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03-26-2013 01:30 PM
Proteinā??protein HADDocking using exclusively pseudocontact shifts
Proteinā??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 Īµ domain of the E. coli DNA polymerase III (Īµ186) 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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11-27-2010 02:45 PM
[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 using paramagnetic metal tags
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