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Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural m...

Moura, José J. G.; Palma, P. Nuno; Lagoutte, Bernard; Krippahl, Ludwig; Guerlesquin, Françoise

FEBS Letters 579 (2005) 4585–4590 ; Abstract Ferredoxin (Fd) and ferredoxin-NADP+-reductase(FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance(NMR)-restrained-docking approach, two alternative structural models of the Fd–FNR complex in the presence of NADP+ are proposed. The protein docking simulations were performed with the softw...

Data: 2005   |   Origem: Repositório Institucional da UNL

A further investigation of the cytochrome b5–cytochrome c complex

Banci, Lucia; Bertini, Ivano; Moura, José J. G.; Felli, Isabella C.; Krippahl, Ludwig; Kubicek, Karel

J Biol Inorg Chem (2003) 8: 777–786 DOI 10.1007/s00775-003-0479-y ; The interaction of reduced rabbit cytochrome b(5) with reduced yeast iso-1 cytochrome c has been studied through the analysis of (1)H-(15)N HSQC spectra, of (15)N longitudinal ( R(1)) and transverse ( R(2)) relaxation rates, and of the solvent exchange rates of protein backbone amides. For the first time, the adduct has been investigated also ...

Data: 2003   |   Origem: Repositório Institucional da UNL

Integrating protein structural information

Krippahl, Ludwig

Dissertação apresentada para obtenção de Grau de Doutor em Bioquímica,Bioquímica Estrutural, pela Universidade Nova de Lisboa, Faculdade de Ciências e Tecnologia ; The central theme of this work is the application of constraint programming and other artificial intelligence techniques to protein structure problems, with the goal of better combining experimental data with structure prediction methods. Part one o...

Data: 2003   |   Origem: Repositório Institucional da UNL

A further investigation of the cytochrome b5–cytochrome c complex

Moura, José J. G.; Banci, Lucia; Bertini, Ivano; Felli, Isabella C.; Krippahl, Ludwig; Kubicek, Karel; Rosato, Antonio

J Biol Inorg Chem (2003) 8: 777–786 ; The interaction of reduced rabbit cytochrome b5 with reduced yeast iso-1 cytochrome c has been studied through the analysis of 1H–15N HSQC spectra, of 15N longitudinal (R1) and transverse (R2) relaxation rates, and of the solvent exchange rates of protein backbone amides. For the first time, the adduct has been investigated also from the cytochrome c side. The analysis of ...

Data: 2003   |   Origem: Repositório Institucional da UNL

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