Measurement of relaxation rates of N(H) and H(alpha) backbone protons in proteins with tailored initial conditions
- Resource Type
- Authors
- Geoffrey Bodenhausen; Oscar Millet; Miquel Pons; Philippe Pelupessy; Elisabetta Chiarparin
- Source
- Journal of magnetic resonance (San Diego, Calif. : 1997). 139(2)
- Subject
- Nuclear and High Energy Physics
Carbon Isotopes
Magnetic Resonance Spectroscopy
Proton
Nitrogen Isotopes
Chemistry
Lysine
Biophysics
Proteins
Condensed Matter Physics
Biochemistry
Homonuclear molecule
Crystallography
chemistry.chemical_compound
Magnetization
Amide
Irradiation
Leucine
Protons
- Language
- ISSN
- 1090-7807
Several methods are presented for the selective determination of spin-lattice and spin-spin relaxation rates of backbone protons in labeled proteins. The relaxation rates of amide protons in (15)N labeled proteins can be measured by using two-way selective cross-polarization (SCP). The measurement of H(alpha) relaxation rates can be achieved by combining this method with homonuclear Hartmann-Hahn transfer using doubly selective irradiation. Various schemes for selective or nonselective inversion of the longitudinal proton magnetization lead to different initial recovery rates. The methods have been applied to lysine K6 in (15)N-labeled human ubiquitin and to leucine L5 in (15)N- and (13)C-labeled octapeptide YG*G*F*LRRI (GFL) in which the marked residues are (15)N- and (13)C-labeled. Copyright 1999 Academic Press. [on SciFinder (R)]