| Literature DB >> 32172451 |
Takayuki Uchihashi1,2, Christian Ganser3,4.
Abstract
Among various microscopic techniques for characterizing protein structures and functions, high-speed atomic force microscopy (HS-AFM) is a unique technique in that it allows direct visualization of structural changes and molecular interactions of proteins without any labeling in a liquid environment. Since the development of the HS-AFM was first reported in 2001, it has been applied to analyze the dynamics of various types of proteins, including motor proteins, membrane proteins, DNA-binding proteins, amyloid proteins, and artificial proteins. This method has now become a versatile tool indispensable for biophysical research. This short review summarizes some bioimaging applications of HS-AFM reported in the last few years and novel applications of HS-AFM utilizing the unique ability of AFM to gain mechanical properties of samples in addition to structural information.Keywords: Conformational dynamics; High-speed atomic force microscopy; Intermolecular interaction; Mechanical indentation; Single-molecule imaging
Year: 2020 PMID: 32172451 PMCID: PMC7242530 DOI: 10.1007/s12551-020-00670-z
Source DB: PubMed Journal: Biophys Rev ISSN: 1867-2450