Abstract: The present disclosure relates to atypical split N- and C-inteins and variants thereof. This disclosure also relates to complexes comprising the split N- or C-inteins of this disclosure and a compound of interest and compositions comprising said complexes. In addition, this disclosure relates to methods of using the atypical split N- and C-inteins.

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: The present invention is a method for accurately comparing the levels of cellular components, such as proteins, present in samples which differ in some respect from each other using mass spectroscopy and isotopic labeling. A first sample of biological matter, such as cells, is cultured in a first medium and a second sample of the same biological matter is cultured in a second medium, wherein at least one isotope in the second medium has a different abundance than the abundance of the same isotope in the first medium. One of the samples is modulated, such as by treatment with a bacteria, a virus, a drug, hormone, a chemical or an environmental stimulus. The samples are combined and at least one protein is removed. The removed protein is subjected to mass spectroscopy to develop a mass spectrum. A ratio is computed between the peak intensities of at least one closely spaced pair of peaks to determine the relative abundance of the protein in each sample.

Abstract: The present invention is a method for accurately comparing the levels of cellular components, such as proteins, present in samples which differ in some respect from each other using mass spectroscopy and isotopic labeling. A first sample of biological matter, such as cells, is cultured in a first medium and a second sample of the same biological matter is cultured in a second medium, wherein at least one isotope in the second medium has a different abundance than the abundance of the same isotope in the first medium. One of the samples is modulated, such as by treatment with a bacteria, a virus, a drug, hormone, a chemical or an environmental stimulus. The samples are combined and at least one protein is removed. The removed protein is subjected to mass spectroscopy to develop a mass spectrum. A ratio is computed between the peak intensities of at least one closely spaced pair of peaks to determine the relative abundance of the protein in each sample.

Abstract: The present invention is a method for accurately comparing the levels of cellular components, such as proteins, present in samples which differ in some respect from each other using mass spectroscopy and isotopic labeling. A first sample of biological matter, such as cells, is cultured in a first medium and a second sample of the same biological matter is cultured in a second medium, wherein at least one isotope in the second medium has a different abundance than the abundance of the same isotope in the first medium. One of the samples is modulated, such as by treatment with a bacteria, a virus, a drug, hormone, a chemical or an environmental stimulus. The samples are combined and at least one protein is removed. The removed protein is subjected to mass spectroscopy to develop a mass spectrum. A ratio is computed between the peak intensities of at least one closely spaced pair of peaks to determine the relative abundance of the protein in each sample.

Abstract: The present invention provides methods for determining the relative orientation of the individual components of a macromolecule in solution with respect to the global molecular coordinate frame of the macromolecule. The present invention further provides methods for applying this structural information, including for rational drug design.

Abstract: The present invention relates to regulation and control of cellular processes by SH3-domain binding proteins and peptides. In particular, the invention provides a consensus sequence of a peptide that shows high specificity and affinity for the first SH3 domain of cellular Crk. In specific examples, a number of peptides that contain the consensus are shown to bind c-Crk specifically. The molecular basis for this specificity is examined by crystallography.

Abstract: A suspension for a pair of wheels of a motor vehicle, comprising a spring (10,30) extending tranversely of the vehicle and supported by two mountings (11,12) spaced between the spring ends and which ends are connected, directly or indirectly, to wheel carrier members, wherein the spring has a portion (22,24) displaced out of the general line of adjacent parts of the spring to give a clearance from a part of the vehicle. The displaced part of the spring may be the entire central portion (40,50,60,100) thereof between its mountings (45,46,101) and end portions of the spring may be inclined to such central portion, so that the space directly between the wheels is clear of suspension parts.

Abstract: A motor vehicle suspension comprising a leaf spring (24) of composite material extending transversely of the vehicle, pivotally supported at two spaced positions (25, 26) between its ends and connected at its ends to wheel carriers, wherein the spring is resiliently supported, at a central region thereof between its pivotal supports, by resilient support means (31, 32, 33, 34) and the bending stiffness of the spring decreases from its pivotal support positions to the central region. The spring is enclosed in a housing (29) between the support positions (25, 26).