title: Investigating fibrillar aggregates of Tau protein by atomic force microscopy.
abstract: Atomic force microscopy (AFM) has been used in numerous studies to visualize and analyze the structure and conformation of biological samples, from single molecules to biopolymers to cells. The possibility to analyze native samples without fixation, staining and in physiological buffer conditions, combined with the sub-nanometer resolution, makes AFM a versatile tool for the analysis of protein aggregation and amyloid structures. Here, we describe the application of AFM to study fibrillar Tau protein aggregates.
authors.affiliation: Department of Biosystems Science and Engineering, ETH Zurich, Basel, Switzerland.
authors.forename: Susanne
authors.initials: S
authors.lastname: Wegmann
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Muller
authors.forename: Eckhard
authors.initials: E
authors.lastname: Mandelkow
mesh_terms: D000327:Adsorption; D000538:Aluminum Silicates / Q000737:chemistry; D005976:Glutaral / Q000737:chemistry; D006801:Humans; D018625:Microscopy, Atomic Force / Q000379:methods*; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D013499:Surface Properties; D013997:Time Factors; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D000538:Aluminum Silicates; D016875:tau Proteins; D005976:Glutaral; C011934:mica