Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites
Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites
Abstract
Pseudocontact shifts (PCS) encode long-range information on 3D structures of protein backbones and side-chains. The level of structural detail that can be obtained increases with the number of different sites tagged with a paramagnetic metal ion to generate PCSs. Here we show that PCSs from two different sites can suffice to determine the structure of polypeptide chains and their location and orientation relative to the magnetic...
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04-24-2017 01:14 AM
Sequence-specific assignment of methyl groups from the neuronal SNARE complex using lanthanide-induced pseudocontact shifts
Sequence-specific assignment of methyl groups from the neuronal SNARE complex using lanthanide-induced pseudocontact shifts
Abstract
Neurotransmitter release depends critically on the neuronal SNARE complex formed by syntaxin-1, SNAP-25 and synaptobrevin, as well as on other proteins such as Munc18-1, Munc13-1 and synaptotagmin-1. Although three-dimensional structures are available for these components, it is still unclear how they are assembled between the synaptic vesicle and plasma membranes to trigger fast, Ca2+-dependent membrane fusion. Methyl...
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12-18-2016 05:04 AM
An encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteins
An encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteins
Abstract
Metal ions serve important roles in structural biology applications from long-range perturbations seen in magnetic resonance experiments to electron-dense signatures in X-ray crystallography data; however, the metal ion must be secured in a molecular framework to achieve the maximum benefit. Polypeptide-based lanthanide-binding tags (LBTs) represent one option that can be directly encoded...
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01-04-2016 07:49 PM
Using Pseudocontact Shifts and Residual Dipolar Couplingsas Exact NMR Restraints for the Determination of Protein StructuralEnsembles
Using Pseudocontact Shifts and Residual Dipolar Couplingsas Exact NMR Restraints for the Determination of Protein StructuralEnsembles
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01138/20151217/images/medium/bi-2015-01138j_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01138
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/-9oN89qR53g
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12-18-2015 07:25 AM
[NMR paper] Using pseudocontact shifts and residual dipolar couplings as exact NMR restraints for the determination of protein structural ensembles.
Using pseudocontact shifts and residual dipolar couplings as exact NMR restraints for the determination of protein structural ensembles.
Using pseudocontact shifts and residual dipolar couplings as exact NMR restraints for the determination of protein structural ensembles.
Biochemistry. 2015 Dec 1;
Authors: Camilloni C, Vendruscolo M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy provides detailed information about the struc-ture and dynamics of proteins by exploiting the conformational dependence of the magnetic...
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12-02-2015 11:37 AM
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 (Î?Ï?) 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
A DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.
A DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.
A DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.
Bioconjug Chem. 2011 Aug 31;
Authors: Graham B, Loh CT, Swarbrick JD, Ung P, Shin J, Yagi H, Jia X, Chhabra S, Barlow N, Pintacuda G, Huber T, Otting G
Abstract
Structural studies of proteins and protein-ligand complexes by nuclear magnetic resonance (NMR) spectroscopy can be greatly enhanced by site-specific attachment of lanthanide ions to...
Three-Dimensional Protein Fold Determination from Backbone Amide Pseudocontact Shifts Generated by Lanthanide ... - ScienceDirect
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