small angle neutron scattering resolution calculator

Kinase (PK) were obtained from Boehringer, valineand GTP, ATP, phosphoenolpyruvate (PEP), and pyruvate Model of the ternary complex different to that described by Macromolecular components and thereby suggests models of Of gyration and on the separation of the centers of mass of the Nucleic acid contributions, information is obtained on the radii By measurement of the scattering curves as the complex is formedĪnd by use of contrast variation to separate protein from Interaction between tRNA and aminoacyl-tRNA synthetases Small-angle neutron scattering (SANS) presents a complementary physical method for studying nucleic acid-proteinĬomplexes which has proved to be successful in studies of the The aminoacyl end of the tRNA interacting with the EF-TuĪnd the two macromolecules being inclined at about 45O to (1981) is a rather open structure with only Model proposed on the basis of low-angle X-ray scattering by Of contact, consistent with the high binding constants foundĥ5$01.50/0 0 1986 American Chemical Societyįor these complexes (Pingoud et al., 1977 Louie et al., 1984 Ībrahamson et al., 1985). Protein and nucleic acid moieties have fairly extensive areas Interaction of the two macromolecular components of theĬomplex (Boutorin et al., 1981 Wikman et al., 1982 Antonsson & Leberman, 1984). A number of chemical and biochemical studies haveīeen described aimed at the determination of the mode of Matic binding of elongator-tRNA to the ribosome-mRNAĬomplex. *Present address: Childrens Hospital of Los Angeles, Los Angeles,

* Author to whom correspondence should be addressed. This complex is then used to promote the enzy. TRNA to produce the ternary complex EF-Tu-GTP-aminoacyl-tRNA. I n bacteria, one of the properties of the soluble polypeptideĮlongation factor Tu (EF-Tu) is to interact with elongator Of the separation of the centers of mass of the protein and t R N A components suggest a compact model The radius of gyration for the ternary complex and the calculation The titration data are then internally consistent with a dissociation of theĭimer on ternary complex formation. Obtained for the protein alone is significantly higher than 'expected and can be explained by postulating a Titrations of the protein with aminoacyl-tRNA solutions in both H 2 0 and 70%D 2 0 confirm the expected stoichiometry. Valyl-tRNAVa' has been studied by small-angle neutron scattering. Received NovemRevised Manuscript Received February 13, 1986ĪBSTRACT: The formation of the ternary complex between bacterial elongation factor Tu, GTP,and Institut h u e - Langevin, 156X, 38042 Grenoble Cedex, France Small-Angle Neutron Scattering Study of the Ternary Complex Formed betweenīacterial Elongation Factor Tu, Guanosine 5'-Triphosphate, and Valyl-tRNAVa1īruno Antonsson,* Reuben Leberman,* and Bernard JacrotĮuropean Molecular Biology Laboratory, 156X. H.-J., Hakoshima, T., van der Marel, G., van Boom, Vorlickova, M., Kypr, J., Kleinwatcher, V., & Palecek, E. H., Weber, H., Koller, T., & Weissman, C. (1984) Principles of Nucleic Acid Structure, Panyutin, I., Lyamichev, V., & Mirkin, S. P., Greiger, I., Eckstein, F., Zarling, D. M., Moller, A., Nordheim, A., Stollar, B.

Kollman, P., Weiner, P., Quigley, G., & Wang, A.

Small angle neutron scattering resolution calculator