2010/06/02 > eTech France 242 > A New Labeling Procedure Pushes the Boundaries of NMR

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		Live from the Lab A New Labeling Procedure Pushes the Boundaries of NMR http://www.bulletins-electroniques.com/actualites/63534.htm Identifying the structure and working of large protein assemblies at the atomic scale is one of today's challenges for biology. Although NMR (Nuclear Magnetic Resonance) is the preferred method for studying the proteins in a solution, its sensitivity is weak and limited to smaller molecules. Pushing these boundaries means resorting to special isotopic protein labeling, an operation involving replacing most of the hydrogen atoms with an isotope, i.e., deuterium, that is invisible in NMR. Only some hydrogen atoms, located in particular positions of the protein, are preserved and visible, thus partially simplifying structure analysis. Grenoble-based researchers at the Jean-Pierre Ebel Structural Biology Institute (Institut de Biologie Structurale Jean-Pierre Ebel, CEA/CNRS/Joseph Fourier University) and at the Laboratory of Metal Chemistry and Biology (Laboratoire de Chimie et Biologie des Métaux, CEA/CNRS/Joseph Fourier University) at the CEA Institute for Research in Life Technologies and Science (Institut de Recherche en Technologies et Sciences pour le Vivant) have developed a new isotopic labeling protocol, to make it even simpler to analyze complex molecular edifices and only label certain hydrogen atoms with more accurate positioning. To do so, they set up and optimized organic synthesis modes making it possible to produce different precursors, specifically enriched in stable isotopes (deuterium and carbon-13). "We can now incorporate 13CH3 methyl groups in a stereo-selective manner into the protein amino acids leucine and valine, and do so directly during their biosynthesis," explained Olivier Hamelin, in charge of the synthesis of the isotopically labeled precursors that can now be used to identify the structure of numerous complex biomolecules. The stereo-selective labeling that substantially increases the quality of NMR data clears the way for numerous applications. Thanks to the improved sensitivity provided by the technique, for the first time the researchers have been able to characterize a particular type of hydrogen linkages in proteins, viz., interactions that have only been predicted theoretically up to now. The new labeling strategy is compatible with the fast NMR techniques recently engineered by the researchers, i.e., techniques which shorten the experimental time for the NMR observation of molecular assemblies of up to one mega Dalton. So, this is a major stride toward the real time observation and atomic resolution of complex biological machinery in action.	>> Suivant << Précédent Version imprimable >> Transmettre cette info par email >> Recommander ce site à un collègue / ami >> S'abonner au eTech France >> FAQ / foire aux questions >> Conditions d'utilisation >>


	Pour en savoir plus, contacts :	Institut de Biologie Structurale Jean-Pierre Ebel (IBS, Structural Biology Institute) - Jérôme Boisbouvier - email: jerome.boisbouvier@ibs.fr	Code brève ADIT : 63534

	Rédacteur :	ADIT - Jean-François Desessard - email: jfd@adit.fr


	Origine :	eTech France numéro 242 (2/06/2010) - ADIT / ADIT - http://www.bulletins-electroniques.com/actualites/63534.htm

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