Band-selective 3D NOESY-TOCSY: Measurement of through-space correlations between aliphatic protons of membrane peptides and proteins in non-deuterated detergents |
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Authors: | Christine Le Guernevé Michel Seigneuret |
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Institution: | (1) Laboratoire de Biophysique Cellulaire et RMN, Université Paris 7-Denis Diderot, 2 Place Jussieu, F-75251 Paris Cédex 05, France |
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Abstract: | Summary Recently the use of band-selective excitation to obtain 1H 2D NMR spectra of membrane peptides and proteins in non-deuterated detergents has been demonstrated Seigneuret, M. and Levy, D. (1995) J. Biomol. NMR, 5, 345–352]. A limitation of the method was the inability to obtain through-space correlation between aliphatic protons. Here, a 3D F3-band-selective NOESY-TOCSY experiment is described that allows such correlations to be observed in the presence of an excess of non-deuterated detergent. Application to the measurement of proximities between aliphatic protons of the membrane peptide mastoparan X solubilized in non-deuterated n-octylglucoside is presented. With this additional experiment, it is now possible to obtain the same amount of structural constraints on membrane peptides and protein in non-deuterated detergent as in deuterated detergent and therefore to perform complete structural studies. |
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Keywords: | Selective excitation 3D homonuclear NMR Membrane proteins Detergents |
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