Related ArticlesNMR investigations of the structural properties of the nodulation protein, NodF, from Rhizobium leguminosarum and its homology with Escherichia coli acyl carrier protein.
FEBS Lett. 1996 Jun 10;388(1):66-72
Authors: Ghose R, Geiger O, Prestegard JH
Heteronuclear NMR methods have been used to elucidate the secondary structure and the general tertiary fold of the protein NodF from Rhizobium leguminosarum. A similarity to acyl carrier proteins of the fatty acid synthase system had been suggested by the presence of a phosphopantetheine prosthetic group and a short stretch of sequence homology near the prosthetic group attachment site. NMR results suggest that the structural homology extends well beyond this region. Both proteins have three well-formed helices which fold in a parallel-antiparallel fashion and a prosthetic group attachment site near the beginning of the second helix.
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Abstract Laboratories often repeatedly determine the structure of a given protein under a variety of conditions, mutations, modifications, or in a number of states. This approach can be cumbersome and tedious. Given then a database of structures, identifiers, and corresponding 1H,15N-HSQC NMR spectra for homologous proteins, we investigated whether structural information could be ascertained for a new homolog solely from its...
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Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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09-30-2011 05:59 AM
Structural, EPR Superhyperfine, and NMR Hyperfine Properties of the Cu-Octarepeat Binding Site in the Prion Protein.
Structural, EPR Superhyperfine, and NMR Hyperfine Properties of the Cu-Octarepeat Binding Site in the Prion Protein.
Structural, EPR Superhyperfine, and NMR Hyperfine Properties of the Cu-Octarepeat Binding Site in the Prion Protein.
J Phys Chem B. 2011 Feb 28;
Authors: Ling Y, Khade RL, Zhang Y
Previous experimental and computational investigations show that the copper binding in the prion protein that is involved in a number of neurodegenerative diseases is complicated and the exact binding structures remain to be determined. To facilitate...
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[NMR paper] Structural investigations of a human calcitonin-derived carrier peptide in a membrane
Structural investigations of a human calcitonin-derived carrier peptide in a membrane environment by solid-state NMR.
Related Articles Structural investigations of a human calcitonin-derived carrier peptide in a membrane environment by solid-state NMR.
Biochemistry. 2004 Oct 5;43(39):12459-68
Authors: Wagner K, Beck-Sickinger AG, Huster D
Previous studies have shown that human calcitonin (hCT) and its C-terminal fragment hCT(9-32) translocate in nasal epithelium. Moreover, hCT(9-32) was used as a carrier to internalize efficiently the green...
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[NMR paper] Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR expe
Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.
Biochemistry. 1997 Jul 22;36(29):8977-91
Authors: Schwalbe H, Fiebig KM, Buck M, Jones JA, Grimshaw SB, Spencer A, Glaser SJ, Smith LJ, Dobson CM
...
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[NMR paper] What function for human lithostathine?: structural investigations by three-dimensiona
What function for human lithostathine?: structural investigations by three-dimensional structure modeling and high-resolution NMR spectroscopy.
Related Articles What function for human lithostathine?: structural investigations by three-dimensional structure modeling and high-resolution NMR spectroscopy.
Protein Eng. 1996 Nov;9(11):949-57
Authors: Patard L, Stoven V, Gharib B, Bontems F, Lallemand JY, De Reggi M
Human lithostathine is a 144-residue protein, expressed in various organs and pathologies. Several biological functions have been...
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Solid-State NMR Reveals Structural and Dynamical Properties of a Membrane Protein
http://pubs.acs.org/cgi-bin/abstract.cgi/jacsat/2007/129/i21/abs/ja069028m.html
Solid-State NMR Reveals Structural and Dynamical Properties of a Membrane-Anchored Electron-Carrier Protein, Cytochrome b<sub>5</sub>
<aui auinm="Durr, U. H. N."> <aui auinm="Yamamoto, K."> <aui auinm="Im, S.-C."> <aui auinm="Waskell, L."> <aui auinm="Ramamoorthy, A."> <aug><aul></aul></aug></aui></aui></aui></aui></aui> <au>Ulrich H. N. Dürr,</au> <au>Kazutoshi Yamamoto,</au><au>Sang-Choul Im,</au><au>Lucy Waskell,and </au><au>Ayyalusamy Ramamoorthy*</au>
*ramamoor@umich.edu
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...
NMR investigations of the structural properties of the nodulation protein, NodF, from
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