title: Protein structural changes induced by their uptake at interfaces.
abstract: 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 to changes involving only the tertiary structure, while for other proteins this environment modification will induce drastic changes such as the unfolding of large domains. The structural transitions are mainly governed by the presence of hydrophobic domains and/or by the existence of induced amphipathic properties.
authors: CRBM-CNRS, UPR 1086, 1919 route de Mende, F-34293 Montpellier Cedex 5, France. heitz@crbm.cnrs-mop.fr
authors: Frédéric
authors: F
authors: Heitz
authors: Nicole
authors: N
authors: Van Mau
mesh_terms: D000327:Adsorption; D000388:Air; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013499:Surface Properties; D014867:Water; D014961:X-Ray Diffraction
chemical_list: D008051:Lipid Bilayers; D011506:Proteins; D014867:Water