Single protein molecule mapping with magnetic atomic force microscopy.

ABSTRACT: Understanding the structural organization and distribution of proteins in biological cells is of fundamental importance in biomedical research. The use of conventional fluorescent microscopy for this purpose is limited due to its relatively low spatial resolution compared to the size of a single protein molecule. Atomic force microscopy (AFM), on the other hand, allows one to achieve single-protein resolution by scanning the cell surface using a specialized ligand-coated AFM tip. However, because this method relies on short-range interactions, it is limited to the detection of binding sites that are directly accessible to the AFM tip. We developed a method based on magnetic (long-range) interactions and applied it to investigate the structural organization and distribution of endothelin re

SUBMITTER: Moskalenko AV 

PROVIDER: S-EPMC2814202 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature