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Transverse Relaxation of Scalar Coupled Protons in Magnetic Resonance of Non-Deuterated Proteins
Authors:Takuya F Segawa  Bikash Baishya  " target="_blank">Geoffrey Bodenhausen
Institution:1.Laboratoire de Résonance Magnétique Biomoléculaire,Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, BCH,Lausanne,Switzerland;2.Département de Chimie,Ecole Normale Supérieure,Paris Cedex 05,France;3.UMPC,Paris,France;4.CNRS, UMR 7203,Paris,France;5.Chemical Physics Department,Weizmann Institute,Rehovot,Israel
Abstract:The transverse relaxation rates R 2 = 1/T 2 of protons can be determined by spin-echo sequences with multiple refocusing pulses using moderate radio-frequency field strengths and properly chosen inter-pulse delays so as to suppress echo modulations due to homonuclear scalar couplings. Combination with 2D heteronuclear correlation spectroscopy (HSQC) allows one to measure R 2 of arbitrary protons attached to nitrogen-15 or carbon-13 nuclei. Decays of six amide protons in the protein Ubiquitin that is nitrogen-15 enriched (but not deuterated) were measured at different temperatures.
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