[NMR paper] NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
Related ArticlesNMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
Methods Mol Biol. 2014;1200:501-9
Authors: Hemmi H
Abstract
One of the most commonly used ligand-based NMR methods for detecting ligand binding is saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy. The STD NMR method is an invaluable technique for assessing carbohydrate-lectin interactions in solution, because STD NMR can be used to detect weak ligand binding (Kd ca. 10(-3)-10(-8) M). STD NMR spectra identify the binding epitope of a carbohydrate ligand when bound to lectin. Further, the STD NMR method uses 1H-detected NMR spectra of only the carbohydrate, and so only small quantities of non-labeled lectin are required. In this chapter, I describe a protocol for the STD NMR method, including the experimental procedures used to acquire, process, and analyze STD NMR data, using STD NMR studies for methyl-?-D-galactopyranoside (?-Me-Gal) binding to the C-terminal domain of an R-type lectin from earthworm (EW29Ch) as an example.
[NMR paper] Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Related Articles Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Anal Bioanal Chem. 2014 Mar 25;
Authors: Yu F, Roy S, Arevalo E, Schaeck J, Wang J, Holte K, Duffner J, Gunay NS, Capila I, Kaundinya GV
Abstract
The binding affinity and specificity of heparin to proteins is widely recognized to be sulfation-pattern dependent. However, for the majority of heparin-binding proteins (HBPs), it still remains...
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03-26-2014 12:44 PM
[NMR paper] Saturation transfer difference NMR for fragment screening.
Saturation transfer difference NMR for fragment screening.
Related Articles Saturation transfer difference NMR for fragment screening.
Curr Protoc Chem Biol. 2013 Dec 1;5(4):251-68
Authors: Begley DW, Moen SO, Pierce PG, Zartler ER
Abstract
Fragment screening by saturation transfer difference nuclear magnetic resonance (STD-NMR) is a robust method for identifying small molecule binders and is well suited to a broad set of biological targets. STD-NMR is exquisitely sensitive for detecting weakly binding compounds (a common characteristic of...
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01-07-2014 11:16 PM
[NMR paper] Specific RNA-protein interactions detected with saturation transfer difference NMR.
Specific RNA-protein interactions detected with saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.landesbioscience.com-icon-pubmed-Landesbioscience2.jpg Specific RNA-protein interactions detected with saturation transfer difference NMR.
RNA Biol. 2013 Jul 30;10(8)
Authors: Harris KA, Shekhtman A, Agris PF
Abstract
RNA, at the forefront of biochemical research due to its central role in biology, is recognized by proteins through various mechanisms. Analysis of the...
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08-21-2013 08:49 PM
[Question from NMRWiki Q&A forum] Saturation transfer difference TROSY
Saturation transfer difference TROSY
Has anyone added a pulse scheme for cross saturation to their TROSY for Bruker platform?
Could you share a pulse sequence if you have one?
Thanks!
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05-18-2013 09:22 AM
[NMR paper] Monomer-collagen interactions studied by saturation transfer difference NMR.
Monomer-collagen interactions studied by saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-sage.gif Related Articles Monomer-collagen interactions studied by saturation transfer difference NMR.
J Dent Res. 2013 Mar;92(3):284-8
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagami J
Abstract
Functional monomers in dentin adhesives are involved in wetting dental substrates, demineralization, and the formation of calcium salts....
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04-09-2013 06:31 PM
[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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12-01-2010 06:56 PM
[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...
NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
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