Arsenical probes enable structural studies of proteins. We report the first organoarsenic probes for nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy to study proteins in solutions. These probes can be attached to irregular loop regions. A lanthanide-binding tag induces sizable pseudocontact shifts in protein NMR spectra of a magnitude never observed for small paramagnetic probes before.
[NMR paper] Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Related Articles Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Nat Commun. 2021 Jan 29;12(1):691
Authors: Nerli S, De Paula VS, McShan AC, Sgourakis NG
Abstract
Methyl-specific isotope labeling is a powerful tool to study the structure, dynamics and interactions of large proteins and protein complexes by solution-state NMR. However, widespread applications of this methodology have been limited by challenges in...
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01-31-2021 02:47 PM
Alpha protons as NMR probes in deuterated proteins
Alpha protons as NMR probes in deuterated proteins
Abstract
We describe a new labeling method that allows for full protonation at the backbone Hα position, maintaining protein side chains with a high level of deuteration. We refer to the method as alpha proton exchange by transamination (α-PET) since it relies on transaminase activity demonstrated here using Escherichia coli expression. We show that α-PET labeling is particularly useful in improving structural characterization of solid proteins by introduction of an additional proton reporter,...
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03-24-2019 10:41 PM
EPR Spectroscopy of Nitroxide Spin Probes #EPR #DNPNMR
From The DNP-NMR Blog:
EPR Spectroscopy of Nitroxide Spin Probes #EPR #DNPNMR
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Nitroxide spin labels are extensively used in EPR for distance measurements and many polarizing agents are based on nitroxides. More recently they are also used in Overhauser DNP measurements (ODNP) to study surface hydration dynamics of larger (membrane) proteins. Although the article is already a bit older, it is a nice review of spin labels and their use in EPR spectroscopy.
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08-14-2017 03:27 PM
[NMR paper] In-cell (13)C NMR spectroscopy for the study of intrinsically disordered proteins.
In-cell (13)C NMR spectroscopy for the study of intrinsically disordered proteins.
In-cell (13)C NMR spectroscopy for the study of intrinsically disordered proteins.
Nat Protoc. 2014 Sep;9(9):2005-2016
Authors: Felli IC, Gonnelli L, Pierattelli R
Abstract
A large number of proteins carry out their function in highly flexible and disordered states, lacking a well-defined 3D structure. These proteins, referred to as intrinsically disordered proteins (IDPs), are now in the spotlight of modern structural biology. Nuclear magnetic...
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08-01-2014 06:21 PM
[NMR paper] Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Molecules. 2013;18(7):7407-7435
Authors: Schrank E, Wagner GE, Zangger K
Abstract
Many peptides and proteins are attached to or immersed in a biological membrane. In order to understand their function not only the structure but also their topology in the membrane is important. Solution NMR spectroscopy is one of the most often...
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
[NMR paper] Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
Related Articles Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
J Am Chem Soc. 2004 Jun 9;126(22):7119-25
Authors: Serber Z, Straub W, Corsini L, Nomura AM, Shimba N, Craik CS, Ortiz de Montellano P, Dötsch V
Studying protein components of large intracellular complexes by in-cell NMR has so far been impossible because the backbone resonances are unobservable due to their slow tumbling rates. We describe a methodology that overcomes...
Organoarsenic probes to study proteins by NMR spectroscopy
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