Тип публикации: статья из журнала
Год издания: 2012
Идентификатор DOI: 10.1016/j.febslet.2012.10.015
Ключевые слова: Bioluminescence, Coelenterazine, Photoprotein, Thermostability, calcium, photoprotein obelin, unclassified drug, article, circular dichroism, ligand binding, priority journal, protein conformation, protein expression, protein function, protein purification, protein stability, protein structure, protein unfolding, structure analysis, Imidazoles, Luminescent Proteins, Protein Binding, Protein Folding, Pyrazines, Spectrometry, Fluorescence
Аннотация: Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism ( CD) data show that the various ligand-dependent conformatioПоказать полностьюnal states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Журнал: FEBS LETTERS
Выпуск журнала: Vol. 586, Is. 23
Номера страниц: 4173-4179
ISSN журнала: 00145793
Место издания: AMSTERDAM
Издатель: ELSEVIER SCIENCE BV