title: Mechanical mapping of single membrane proteins at submolecular resolution.
abstract: The capacity of proteins to carry out different functions is related to their ability to undergo conformation changes, which depends on the flexibility of protein structures. In this work, we applied a novel imaging mode based on indentation force spectroscopy to map quantitatively the flexibility of individual membrane proteins in their native, folded state at unprecedented submolecular resolution. Our results enabled us to correlate protein flexibility with crystal structure and showed that α-helices are stiff structures that may contribute importantly to the mechanical stability of membrane proteins, while interhelical loops appeared more flexible, allowing conformational changes related to function.
authors.affiliation: Institut Curie, U1006 INSERM, 26 rue d'Ulm, 75005 Paris, France.
authors.forename: Felix
authors.initials: F
authors.lastname: Rico
authors.forename: Chanmin
authors.initials: C
authors.lastname: Su
authors.forename: Simon
authors.initials: S
authors.lastname: Scheuring
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry*; D003460:Crystallization; D004548:Elasticity; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D018625:Microscopy, Atomic Force / Q000379:methods; D036103:Nanotechnology / Q000379:methods; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000032:analysis* / Q000737:chemistry
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins; D011506:Proteins; D001436:Bacteriorhodopsins