Related ArticlesBackbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Protein Sci. 2003 Sep;12(9):2104-8
Authors: Liu W, Rumbley J, Englander SW, Wand AJ
The [H26N, H33N] mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2)) states of the protein were obtained using standard triple resonance and total correlation spectroscopy using the previously determined (1)H chemical shifts of the wild-type protein as a guide. The correspondence of chemical shifts between the wild type and the mutant protein is excellent, indicating that they have nearly identical structures. The expanded library of chemical shifts for both redox states in both proteins allowed the refinement of the electron spin g-tensor of the oxidized states. The g-tensors of the oxidized states of the wild-type and [H26N, H33N] mutant proteins are closely similar, indicating that the subtle details of the ligand fields are nearly identical. The refined g-tensors were then used to probe for redox-dependent structure change in the two proteins.
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.
Biomol NMR Assign. 2011 Jul 6;
Authors: Veith T, Wurm JP, Duchardt-Ferner E, Weis B, Martin R, Safferthal C, Bohnsack MT, Schleiff E, Wöhnert J
Eukaryotic ribosome biogenesis requires the concerted action of ~200 auxiliary protein factors on the nascent ribosome. For many of these...
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Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
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[NMR paper] Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic t
Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
Related Articles Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
J Biomol NMR. 2005 Apr;31(4):279-93
Authors: Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ
This study reports the sequence specific chemical shifts...
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[NMR paper] Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 doma
Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla.
Related Articles Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla.
Chembiochem. 2001 Apr 2;2(4):272-81
Authors: Pauli J, Baldus M, van Rossum B, de Groot H, Oschkinat H
The backbone and side-chain 13C and 15N signals of a solid 62-residue (u-13C,15N)-labelled protein containing the alpha-spectrin SH3 domain were...
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11-19-2010 08:32 PM
[NMR paper] Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain
Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
Related Articles Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
J Chem Inf Comput Sci. 1997 May-Jun;37(3):467-77
Authors: Li KB, Sanctuary BC
A sequential assignment protocol for proteins was developed using heteronuclear 3D NMR. The protocol consists of an amino acid type recognition algorithm and a primary sequence mapping algorithm. The former measures...
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08-22-2010 03:31 PM
[NMR paper] Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain
Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
Related Articles Automated resonance assignment of proteins using heteronuclear 3D NMR. 2. Side chain and sequence-specific assignment.
J Chem Inf Comput Sci. 1997 May-Jun;37(3):467-77
Authors: Li KB, Sanctuary BC
A sequential assignment protocol for proteins was developed using heteronuclear 3D NMR. The protocol consists of an amino acid type recognition algorithm and a primary sequence mapping algorithm. The former measures...
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08-22-2010 03:03 PM
[NMR paper] Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in
Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy.
Related Articles Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy.
Biochemistry. 1991 Sep 24;30(38):9216-28
Authors: Ikura M, Spera S, Barbato G, Kay LE, Krinks M, Bax A
Heteronuclear 2D and 3D NMR experiments were carried out on recombinant Drosophila calmodulin (CaM), a protein of 148 residues and with...
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08-21-2010 11:12 PM
[NMR paper] Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in
Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy.
Related Articles Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy.
Biochemistry. 1991 Sep 24;30(38):9216-28
Authors: Ikura M, Spera S, Barbato G, Kay LE, Krinks M, Bax A
Heteronuclear 2D and 3D NMR experiments were carried out on recombinant Drosophila calmodulin (CaM), a protein of 148 residues and with...