title: Single-molecule studies of membrane proteins.
abstract: Characterizing membrane proteins with single-molecule techniques provides structural and functional insights that cannot be obtained with conventional approaches. Recent studies show that atomic force microscopy (AFM) in the context of a 'lab on a tip' enables the measurement of multiple parameters of membrane proteins. This multifunctional tool can be applied to probe the oligomeric states and conformational changes of membrane protein assemblies in their native environment. The ability to determine diverse properties at high spatial resolution facilitates the mapping of structural flexibilities, electrostatic potentials and electric currents. By using the AFM tip as tweezer, it is possible to characterize unfolding and refolding pathways of single proteins and the location of their molecular interactions. These interactions dictate the stability of the protein and might be modulated by ligands that alter the protein's functional state.
authors.affiliation: Center for Biotechnology, University of Technology, 01307 Dresden, Germany. mueller@biotec.tu-dresden.de
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Müller
authors.forename: K Tanuj
authors.initials: KT
authors.lastname: Sapra
authors.forename: Simon
authors.initials: S
authors.lastname: Scheuring
authors.forename: Alexej
authors.initials: A
authors.lastname: Kedrov
authors.forename: Patrick L
authors.initials: PL
authors.lastname: Frederix
authors.forename: Dimitrios
authors.initials: D
authors.lastname: Fotiadis
authors.forename: Andreas
authors.initials: A
authors.lastname: Engel
mesh_terms: D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D017510:Protein Folding
chemical_list: D008565:Membrane Proteins