High-pressure as a tool to study some proteins properties: conformational modification, activity and oligomeric dissociation
2002
Lullien Pellerin, Valerie | Balny, C. | Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE) ; Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro) | Enzymologie : mécanismes moléculaires et contrôle génétique ; Institut National de la Santé et de la Recherche Médicale (INSERM)
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Mostrar más [+] Menos [-]Inglés. Hydrostatic pressure, as temperature, constitutes an efficient physical parameter to modify equilibrium and rate of biological processes. In this review, we will not present all the implications of high-pressure, but we will focus on proteins’ structural conformational modification, unfolding, oligomeric or protein aggregates dissociation and enzymatic activity. To this aim, some optical methods that were used in association with high-pressure to study protein structures (i.e. fourth derivative absorbance spectroscopy, fluorescence spectroscopy, infrared spectroscopy) and protein activities (kinetics measurements: stopped-flow and pressure jump methods) will be described in details. Some applications of these methods will be given including effects on proteins of food interest.
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