Protein structural changes induced by their uptake at interfaces.
作者： Frédéric Heitz , Nicole Van Mau
DOI: 10.1016/S0167-4838(02)00273-X
关键词: Protein tertiary structure 、 Crystallography 、 Circular dichroism 、 Nuclear magnetic resonance spectroscopy 、 Protein folding 、 Amphiphile 、 Lipid bilayer 、 Protein structure 、 Chemistry 、 Biophysics
摘要: For insertion into lipidic media, most hydrosoluble proteins must cross the lipid-water interface and thus undergo conformational transitions. According to their chemical sequences these transitions may be restricted changes involving only tertiary structure, while for other this environment modification will induce drastic such as unfolding of large domains. The structural are mainly governed by presence hydrophobic domains and/or existence induced amphipathic properties.
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