Mobility is a common feature of biomacromolecules, often fundamental for their function. Thus, in many cases, biomacromolecules cannot be described by a single conformation, but rather by a conformational ensemble. NMR paramagnetic data demonstrated quite informative to monitor this conformational variability, especially when used in conjunction with data from different sources. Due to their long-range nature, paramagnetic data can, for instance, i) clearly demonstrate the occurrence of...
[NMR paper] Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements.
Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements.
Related Articles Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements.
Proteins. 2016 Aug 2;
Authors: Kilpatrick AM, Honts JE, Sleister HM, Fowler CA
Abstract
Tcb2 is a calcium-binding protein that localizes to the membrane-associated skeleton of the ciliated protozoan Tetrahymena thermophila with...
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08-05-2016 12:26 PM
[NMR paper] NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Related Articles NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Protein Sci. 2016 Jan 8;
Authors: Mohanty B, Geralt M, Wüthrich K, Serrano P
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence...
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01-11-2016 03:57 PM
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes...
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01-09-2016 04:06 PM
[NMR paper] Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints.
Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints.
Related Articles Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints.
Curr Opin Struct Biol. 2014 Feb;24C:45-53
Authors: Hass MA, Ubbink M
Abstract
Paramagnetic NMR spectroscopy has evolved rapidly in the last decade, and has shown to be a very useful tool for solving structures of protein-protein complexes. A major breakthrough has been the development of...
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04-12-2014 06:36 PM
Structure determination of protein–protein complexes with long-range anisotropic paramagnetic NMR restraints
Structure determination of protein–protein complexes with long-range anisotropic paramagnetic NMR restraints
Publication date: February 2014
Source:Current Opinion in Structural Biology, Volume 24</br>
Author(s): Mathias AS Hass , Marcellus Ubbink</br>
Paramagnetic NMR spectroscopy has evolved rapidly in the last decade, and has shown to be a very useful tool for solving structures of protein–protein complexes. A major breakthrough has been the development of paramagnetic metal binding tags that can be attached specifically to the protein. These tags have greatly...
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12-21-2013 03:15 PM
[NMR paper] Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon
Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
Related Articles Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
Int J Biol Macromol. 2003 Dec;33(4-5):193-201
Authors: Cicero DO, Melino S, Orsale M, Brancato G, Amadei A,...
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[NMR paper] Structural characterization of proteins with an attached ATCUN motif by paramagnetic
Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.
Related Articles Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.
J Am Chem Soc. 2001 Oct 10;123(40):9843-7
Authors: Donaldson LW, Skrynnikov NR, Choy WY, Muhandiram DR, Sarkar B, Forman-Kay JD, Kay LE
The use of a short, three-residue Cu(2+)-binding sequence, the ATCUN motif, is presented as an approach for extracting long-range distance...
Paramagnetic NMR restraints for the characterization of protein structural rearrangements
Linear Mode
