Related ArticlesA novel NMR method for determining the interfaces of large protein-protein complexes.
Nat Struct Biol. 2000 Mar;7(3):220-3
Authors: Takahashi H, Nakanishi T, Kami K, Arata Y, Shimada I
Identification of the interfaces of large (Mr > 50,000) protein-protein complexes in solution by high resolution NMR has typically been achieved using experiments involving chemical shift perturbation and/or hydrogen-deuterium exchange of the main chain amide groups of the proteins. Interfaces identified using these techniques, however, are not always identical to those revealed using X-ray crystallography. In order to identify the contact residues in a large protein-protein complex more accurately, we developed a novel NMR method that uses cross-saturation phenomena in combination with TROSY detection in an optimally deuterium labeled system.
[NMR paper] High-throughput inference of protein-protein interfaces from unassigned NMR data.
High-throughput inference of protein-protein interfaces from unassigned NMR data.
Related Articles High-throughput inference of protein-protein interfaces from unassigned NMR data.
Bioinformatics. 2005 Jun;21 Suppl 1:i292-301
Authors: Mettu RR, Lilien RH, Donald BR
SUMMARY: We cast the problem of identifying protein-protein interfaces, using only unassigned NMR spectra, into a geometric clustering problem. Identifying protein-protein interfaces is critical to understanding inter- and intra-cellular communication, and NMR allows the study of...
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[NMR paper] An NMR method for the determination of protein-binding interfaces using dioxygen-indu
An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
Related Articles An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
J Am Chem Soc. 2005 Apr 27;127(16):5826-32
Authors: Sakakura M, Noba S, Luchette PA, Shimada I, Prosser RS
Using oxygen as a paramagnetic probe, researchers can routinely study topologies and protein-binding interfaces by NMR. The paramagnetic contribution to the amide (1)H...
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[NMR paper] Rapid analysis of large protein-protein complexes using NMR-derived orientational con
Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein.
Related Articles Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein.
J Mol Biol. 2004 Nov 5;343(5):1379-89
Authors: Jain NU, Wyckoff TJ, Raetz CR, Prestegard JH
Characterization of protein-protein interactions that are critical to the specific function of many biological systems has become a primary...
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[NMR paper] SOS-NMR: a saturation transfer NMR-based method for determining the structures of pro
SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes.
Related Articles SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes.
J Am Chem Soc. 2004 Mar 3;126(8):2390-8
Authors: Hajduk PJ, Mack JC, Olejniczak ET, Park C, Dandliker PJ, Beutel BA
An NMR-based alternative to traditional X-ray crystallography and NMR methods for structure-based drug design is described that enables the structure determination of ligands complexed to virtually...
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[NMR paper] Determining the structures of large proteins and protein complexes by NMR.
Determining the structures of large proteins and protein complexes by NMR.
Related Articles Determining the structures of large proteins and protein complexes by NMR.
Trends Biotechnol. 1998 Jan;16(1):22-34
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR methodology to obtain 1H, 15N and 13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structure of proteins in excess...
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Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Angew Chem Int Ed Engl. 2010 Jul 29;
Authors: Zhu J, Ye E, Terskikh V, Wu G
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Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Angew Chem Int Ed Engl. 2010 Jul 28;
Authors: Zhu J, Ye E, Terskikh V, Wu G
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HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections
HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections
Gabriel Cornilescu, Arash Bahrami, Marco Tonelli, John L. Markley and Hamid R. Eghbalnia
Journal of Biomolecular NMR; 2007; 38(4); pp 341-351
Abstract:
We describe a novel method for the robust, rapid, and reliable determination of J couplings in multi-dimensional NMR coupling data, including small couplings from larger proteins. The method, “High-resolution Iterative Frequency Identification of Couplings” (HIFI-C) is an extension of the adaptive and intelligent data collection approach...