Publication date: 3 February 2017 Source:Biophysical Journal, Volume 112, Issue 3, Supplement 1
Author(s): Adina M. Kilpatrick, Jerry E. Honts, Heidi M. Sleister, C. Andrew Fowler
[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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NMR Structural Studies of the C-Domain of Tcb2, A Calcium Binding Protein from Tetrahymena Thermophila
NMR Structural Studies of the C-Domain of Tcb2, A Calcium Binding Protein from Tetrahymena Thermophila
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Adina M. Kilpatrick, C. Andrew Fowler, Theodore Gurrola, Jerry E. Honts</br>
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[NMR paper] Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Related Articles Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Biochemistry. 2015 Nov 30;
Authors: Kukic P, Lundström P, Camilloni C, Evenäs J, Akke M, Vendruscolo M
Abstract
Calmodulin is a two-domain signalling protein that becomes activated upon binding cooperatively two pairs of calcium ions, leading to large-scale...
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Fluorescence Microscopy and Solution NMR Studies of Cytoskeletal Proteins from Tetrahymena
Fluorescence Microscopy and Solution NMR Studies of Cytoskeletal Proteins from Tetrahymena
Publication date: 27 January 2015
Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1</br>
Author(s): Robert Sterner , Jerry Honts , Adina Kilpatrick</br>
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Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
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[NMR paper] Calcium-induced peptide association to form an intact protein domain: 1H NMR structur
Calcium-induced peptide association to form an intact protein domain: 1H NMR structural evidence.
Related Articles Calcium-induced peptide association to form an intact protein domain: 1H NMR structural evidence.
Science. 1990 Jul 20;249(4966):280-3
Authors: Shaw GS, Hodges RS, Sykes BD
The 70-residue carboxyl-terminal domain of the muscle contractile protein troponin-C contains two helix-loop-helix calcium (Ca)-binding sites that are related to each other by approximate twofold rotational symmetry. Hydrophobic residues from the helices and a...