caa a22 4500 44532578X CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110701xx s 000 0 eng 10.1007/s10858-011-9510-8 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9510-8 Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein [Elektronische Daten] [Rafal Augustyniak, Fabien Ferrage, Raphaël Paquin, Olivier Lequin, Geoffrey Bodenhausen] We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion delay as longitudinal polarization of nuclei with long T1 such as nitrogen-15. The new BEST-XSTE sequence combines features of Band-selective Excitation Short-Transient (BEST) and XSTE methods. By avoiding the saturation of all protons except those of amide groups, one can increase the sensitivity by 45% in small proteins. The new experiment which combines band-Selective Optimized Flip-Angle Short-Transient with XSTE (SOFAST-XSTE) offers an alternative when very short recovery delays are desired. A modification of the HSQC-edited version of the XSTE experiment offers enhanced sensitivity and access to higher resolution in the indirect dimension. These new methods have been applied to detect changes in diffusion coefficients due to dimerization or proteolysis of Engrailed 2, a partially disordered protein. Springer Science+Business Media B.V., 2011 Translational diffusion nationallicence Heteronuclear stimulated echoes nationallicence Proteolysis nationallicence Dimerization nationallicence Disulfide bonds nationallicence Partially disordered proteins nationallicence Augustyniak Rafal Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut Ferrage Fabien Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut Paquin Raphaël Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut Lequin Olivier Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut Bodenhausen Geoffrey Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut Journal of Biomolecular NMR Springer Netherlands 50/3(2011-07-01), 209-218 0925-2738 50:3<209 2011 50 10858 https://doi.org/10.1007/s10858-011-9510-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9510-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Augustyniak Rafal Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut NATIONALLICENCE 700 1- Ferrage Fabien Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut NATIONALLICENCE 700 1- Paquin Raphaël Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut NATIONALLICENCE 700 1- Lequin Olivier Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut NATIONALLICENCE 700 1- Bodenhausen Geoffrey Département de chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris Cedex 05, France aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/3(2011-07-01), 209-218 0925-2738 50:3<209 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer