title: Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy.
abstract: Molecular interactions are the basic language of biological processes. They establish the forces interacting between the building blocks of proteins and other macromolecules, thus determining their functional roles. Because molecular interactions trigger virtually every biological process, approaches to decipher their language are needed. Single-molecule force spectroscopy (SMFS) has been used to detect and characterize different types of molecular interactions that occur between and within native membrane proteins. The first experiments detected and localized molecular interactions that stabilized membrane proteins, including how these interactions were established during folding of alpha-helical secondary structure elements into the native protein and how they changed with oligomerization, temperature, and mutations. SMFS also enables investigators to detect and locate molecular interactions established during ligand and inhibitor binding. These exciting applications provide opportunities for studying the molecular forces of life. Further developments will elucidate the origins of molecular interactions encoded in their lifetimes, interaction ranges, interplay, and dynamics characteristic of biological systems.
authors.affiliation: Department of Cellular Machines, Center of Biotechnology, Technische Universität Dresden, 01307 Dresden, Germany.
authors.forename: Alexej
authors.initials: A
authors.lastname: Kedrov
authors.forename: Harald
authors.initials: H
authors.lastname: Janovjak
authors.forename: K Tanuj
authors.initials: KT
authors.lastname: Sapra
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Müller
mesh_terms: D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000737:chemistry; D001671:Biochemistry / Q000379:methods; D001703:Biophysics / Q000379:methods; D007700:Kinetics; D008024:Ligands; D008055:Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods*; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis / Q000379:methods*; D013329:Structure-Activity Relationship
chemical_list: D008024:Ligands; D008055:Lipids; D008565:Membrane Proteins; D001436:Bacteriorhodopsins