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Proceedings of the National Academy of Sciences of the United States of America|March 1, 1974
The lac repressor protein: molecular shape, subunit structure, and proposed model for operator interaction based on structural studies of microcrystalsT A Steitz, T J Richmond, D Wise, et al.
The EMBO Journal|August 15, 1994
The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolutionJ Czworkowski, J Wang, T A Steitz, et al.
European Journal of Biochemistry|April 17, 1978
X-ray and neutron small-angle scattering studies of the complex between protein S1 and the 30-S ribosomal subunitM Laughrea, D M Engelman, P B Moore
The Journal of Biological Chemistry|December 5, 1986
Preliminary X-ray diffraction studies of the putative catalytic domain of gamma delta resolvase from Escherichia coliS S Abdel-Meguid, H M Murthy, T A Steitz
Journal of Biomolecular Structure & Dynamics|December 1, 1983
Crystallographic studies of protein-nucleic acid interaction: catabolite gene activator protein and the large fragment of DNA polymerase IT A Steitz, I T Weber, D Ollis, et al.
The EMBO Journal|November 1, 1986
Reformation of crystalline purple membrane from purified bacteriorhodopsin fragmentsJ L Popot, J Trewhella, D M Engelman
Biophysical Journal|September 1, 1983
Neutron diffraction analysis of cytochrome b5 reconstituted in deuterated lipid multilayersE P Gogol, D M Engelman, G Zaccai
Proceedings of the National Academy of Sciences of the United States of America|August 2, 2001
The Calpha ---H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactionsA Senes, I Ubarretxena-Belandia, D M Engelman
Journal of Molecular Biology|December 5, 1985
Electrostatic field of the large fragment of Escherichia coli DNA polymerase IJ Warwicker, D Ollis, F M Richards, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1982
The cAMP-binding domains of the regulatory subunit of cAMP-dependent protein kinase and the catabolite gene activator protein are homologousI T Weber, K Takio, K Titani, et al.
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