NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein

Autor: Federico Fogolari, Laura Ragona, Jefferson Foote, Maddalena Catalano, Henriette Molinari, Marianna Luppi, Daniel O. Cicero, Tommaso Eliseo, Lucia Zetta

Publikováno v: The Journal of biological chemistry
281 (2006): 9697–9709. doi:10.1074/jbc.M513003200
info:cnr-pdr/source/autori:Ragona L; Catalano M; Luppi M; Cicero D; Eliseo T; Foote J; Fogolari F; Zetta L; Molinari H/titolo:NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein/doi:10.1074%2Fjbc.M513003200/rivista:The Journal of biological chemistry (Print)/anno:2006/pagina_da:9697/pagina_a:9709/intervallo_pagine:9697–9709/volume:281

Apo chicken liver bile acid-binding protein has been structurally characterized by NMR. The dynamic behavior of the protein in its apo- and holo-forms, complexed with chenodeoxycholate, has been determined via (15)N relaxation and steady state hetero

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http://www.cnr.it/prodotto/i/54290