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Results: 1-9 |
Results: 9
Non-covalent interactions in the crystallization of the enantiomers of 1,7-dioxaspiro[5.5]undecane (olive fly sex pheromone) by enantiospecific cyclodextrin hosts, hexakis(2,3,6-tri-O-methyl)-alpha-cyclodextrin and heptakis(2,3,6-tri-O-methyl)-beta-cyclodextrin
Authors: Makedonopoulou, S Yannakopoulou, K Mentzafos, D Lamzin, V Popov, A Mavridis, IM
Citation: S. Makedonopoulou et al., Non-covalent interactions in the crystallization of the enantiomers of 1,7-dioxaspiro[5.5]undecane (olive fly sex pheromone) by enantiospecific cyclodextrin hosts, hexakis(2,3,6-tri-O-methyl)-alpha-cyclodextrin and heptakis(2,3,6-tri-O-methyl)-beta-cyclodextrin, ACT CRYST B, 57, 2001, pp. 399-409
Detailed analysis of RNA-protein interactions within the ribosomal proteinS8-rRNA complex from the archaeon Methanococcus jannaschii
Authors: Tishchenko, S Nikulin, A Fomenkova, N Nevskaya, N Nikonov, O Dumas, P Moine, H Ehresmann, B Ehresmann, C Piendl, W Lamzin, V Garber, M Nikonov, S
Citation: S. Tishchenko et al., Detailed analysis of RNA-protein interactions within the ribosomal proteinS8-rRNA complex from the archaeon Methanococcus jannaschii, J MOL BIOL, 311(2), 2001, pp. 311-324
On the mechanism of biological methane formation: Structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding
Authors: Grabarse, W Mahlert, F Duin, EC Goubeaud, M Shima, S Thauer, RK Lamzin, V Ermler, U
Citation: W. Grabarse et al., On the mechanism of biological methane formation: Structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding, J MOL BIOL, 309(1), 2001, pp. 315-330
Transthyretin stability as a key factor in amyloidogenesis: X-ray analysisat atomic resolution
Authors: Sebastiao, MP Lamzin, V Saraiva, MJ Damas, AM
Citation: Mp. Sebastiao et al., Transthyretin stability as a key factor in amyloidogenesis: X-ray analysisat atomic resolution, J MOL BIOL, 306(4), 2001, pp. 733-744
Accurate protein crystallography at ultra-high resolution: Valence electron distribution in crambin
Authors: Jelsch, C Teeter, MM Lamzin, V Pichon-Pesme, V Blessing, RH Lecomte, C
Citation: C. Jelsch et al., Accurate protein crystallography at ultra-high resolution: Valence electron distribution in crambin, P NAS US, 97(7), 2000, pp. 3171-3176
Structural basis for substrate specificity differences of horse liver alcohol dehydrogenase isozymes
Authors: Adolph, HW Zwart, P Meijers, R Hubatsch, I Kiefer, M Lamzin, V Cedergren-Zeppezauer, E
Citation: Hw. Adolph et al., Structural basis for substrate specificity differences of horse liver alcohol dehydrogenase isozymes, BIOCHEM, 39(42), 2000, pp. 12885-12897
Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 angstrom) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core
Authors: Declercq, JP Evrard, C Lamzin, V Parello, J
Citation: Jp. Declercq et al., Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 angstrom) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core, PROTEIN SCI, 8(10), 1999, pp. 2194-2204
Ab initio structure solution of a dimeric cytochrome c(3) from Desulfovibrio gigas containing disulfide bridges
Authors: Frazao, C Sieker, L Sheldrick, G Lamzin, V LeGall, J Carrondo, MA
Citation: C. Frazao et al., Ab initio structure solution of a dimeric cytochrome c(3) from Desulfovibrio gigas containing disulfide bridges, J BIOL I CH, 4(2), 1999, pp. 162-165
Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution
Authors: Parisini, E Capozzi, F Lubini, P Lamzin, V Luchinat, C Sheldrick, GM
Citation: E. Parisini et al., Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution, ACT CRYST D, 55, 1999, pp. 1773-1784
Risultati: 1-9 |