Abstract: A method for carrying out two-field nuclear magnetic resonance (=2FNMR) measurements involves preparing a sample (9a) in a first working volume (5) of a highly homogeneous magnetic field with a first field strength; transferring the sample (9a) to a second working volume (7) with a magnetic field having lower homogeneity and having a second field strength, wherein the first field strength is at least 2 Tesla larger than the second field strength; manipulating the sample (9a) at the second working volume (7) by applying a sequence of radio-frequency (=RF) and/or field gradient pulses; transferring the sample (9a) back to the first working volume (5); and detecting an NMR signal of the sample (9a) in the first working volume (5). The method allows for NMR experiments with which more and/or improved quality information about an investigated sample can be obtained.

Abstract: A method for carrying out two-field nuclear magnetic resonance (=2FNMR) measurements involves preparing a sample (9a) in a first working volume (5) of a highly homogeneous magnetic field with a first field strength; transferring the sample (9a) to a second working volume (7) with a magnetic field having lower homogeneity and having a second field strength, wherein the first field strength is at least 2 Tesla larger than the second field strength; manipulating the sample (9a) at the second working volume (7) by applying a sequence of radio-frequency (=RF) and/or field gradient pulses; transferring the sample (9a) back to the first working volume (5); and detecting an NMR signal of the sample (9a) in the first working volume (5). The method allows for NMR experiments with which more and/or improved quality information about an investigated sample can be obtained.

Abstract: A method for characterizing interactions in macromolecular complexes, such as protein-protein or protein-ligand complexes, by selective isotopic labeling of the target molecule to reduce the 1H density in a selected spectral region; by irradiating the target; and by monitoring the polarization using filtered nuclear Overhauser spectroscopy (NOESY) and/or by performing selective saturation transfer experiments to determine the docking potential of the macromolecular complex.

Abstract: A pulsed field gradient NMR (=nuclear magnetic resonance) method using stimulated echoes for determining the translational isotropic or anisotropic diffusion coefficient of a molecule or supra-molecular assembly or the flow rate and direction of fluids containing such molecules is characterized in that the molecule or supra-molecular assembly contains one or several isotopes (X) of non-zero nuclear spin other than protons having longitudinal relaxation times T1(X) that are longer than the longitudinal relaxation times T1(H) of the protons, and that the information about the localization of the molecule or supra-molecular assembly during the diffusion or flow interval is temporarily stored in the form of longitudinal magnetization of said isotope or isotopes. Thus, the determination of translational diffusion coefficients or flow rates of supra-molecular assemblies or molecules with short T1(H) values, in particular of supra-molecular assemblies or molecules with M≧50 kDa is accomplished.

Abstract: A pulsed field gradient NMR (=nuclear magnetic resonance) method using stimulated echoes for determining the translational isotropic or anisotropic diffusion coefficient of a molecule or supra-molecular assembly or the flow rate and direction of fluids containing such molecules is characterized in that the molecule or supra-molecular assembly contains one or several isotopes (X) of non-zero nuclear spin other than protons having longitudinal relaxation times T1(X) that are longer than the longitudinal relaxation times T1(H) of the protons, and that the information about the localization of the molecule or supra-molecular assembly during the diffusion or flow interval is temporarily stored in the form of longitudinal magnetization of said isotope or isotopes. Thus, the determination of translational diffusion coefficients or flow rates of supra-molecular assemblies or molecules with short T1(H) values, in particular of supra-molecular assemblies or molecules with M≧50 kDa is accomplished.