Related ArticlesDissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.
J Magn Reson. 2003 Nov;165(1):89-94
Authors: Braun D, Wüthrich K, Wider G
Modern NMR experiments for applications with biological macromolecules in solution typically include multiple magnetization transfer steps. When working with large structures, a significant fraction of the magnetization is lost during these transfers. For the design and optimization of complex experimental schemes, the magnetization transfer efficiencies have therefore commonly been calculated from the spin relaxation times. This paper now suggests a new method for measurement of individual transfer efficiencies directly with the system of interest, using short, reliable experiments. Initial applications of this approach with a 110,000 Da protein indicate that there is a wide range of transfer efficiencies among individual spin pairs in a structure of this size, which leads to a correspondingly large variation of the individual signal intensities and the need for techniques to enhance the weak signals.
[NMR paper] Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experim
Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Related Articles Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Proteins. 2004 Aug 1;56(2):346-53
Authors: Haselhorst T, Wilson JC, Thomson RJ, McAtamney S, Menting JG, Coppel RL, von Itzstein M
Saturation transfer difference...
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Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed int
Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein-peptide interactions.
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Chem Commun (Camb). 2010 Sep 13;
Authors: Wagstaff JL, Vallath S, Marshall JF, Williamson RA, Howard MJ
We report the first example of peptide-protein heteronuclear two-dimensional (2D) saturation transfer difference nuclear magnetic resonance (STD NMR). This method, resulting in...
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[NMR paper] Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of
Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
Eur J Biochem. 1996 Feb 1;235(3):699-712
Authors: Krebs D, Dahmani B, Monnot M, Mauffret O,...
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[NMR paper] 19F NMR magnetization transfer between 5-FBAPTA and its complexes. An alternative mea
19F NMR magnetization transfer between 5-FBAPTA and its complexes. An alternative means for measuring free Ca2+ concentration, and detection of complexes with protein in erythrocytes.
Related Articles 19F NMR magnetization transfer between 5-FBAPTA and its complexes. An alternative means for measuring free Ca2+ concentration, and detection of complexes with protein in erythrocytes.
NMR Biomed. 1994 Nov;7(7):330-8
Authors: Gilboa H, Chapman BE, Kuchel PW
The 19F NMR Ca(2+)-indicator molecule 5,5'-difluoro-1,2-bis(o-...
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[NMR paper] Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments.
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Biochemistry. 1992 Aug 25;31(33):7741-4
Authors: Mott HR, Driscoll PC, Boyd J, Cooke RM, Weir MP, Campbell ID
Recombinant 15N-labeled human interleukin 2 (IL-2) has been studied by 2D and 3D NMR using uniformly 15N-labeled protein. Assignment of the backbone resonances has enabled the secondary structure of the protein to be defined. The secondary structure was...
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[NMR paper] Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: s
Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure.
Related Articles Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure.
Biochemistry. 1991 Dec 10;30(49):11600-8
Authors: Simorre JP, Caille A, Marion D, Marion D, Ptak M
Two- and three-dimensional 1H NMR experiments have been used to sequentially assign nearly all proton resonances of the 90 residues of wheat...
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Broadband Heteronuclear Solid-State NMR Experiments by Exponentially Modulated Dipola
Broadband Heteronuclear Solid-State NMR Experiments by Exponentially Modulated Dipolar Recoupling without Decoupling.
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J Phys Chem Lett. 2010 Jun 1;1(13):1952-1956
Authors: Nielsen AB, Straasø LA, Nieuwkoop AJ, Rienstra CM, Bjerring M, Nielsen NC
We present a novel solid-state NMR method for...
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Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins
Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins
W. Trent Franks, Kathryn D. Kloepper, Benjamin J. Wylie and Chad M. Rienstra
Journal of Biomolecular NMR; 2007; 39(2); pp 107 - 131
Abstract:
Chemical shift assignment is the first step in all established protocols for structure determination of uniformly labeled proteins by NMR. The explosive growth in recent years of magic-angle spinning (MAS) solid-state NMR (SSNMR) applications is largely attributable to improved methods for backbone and side-chain chemical shift correlation...