Abstract
Atomic force microscopy (AFM) has demonstrated ability to provide direct visualization of individual molecules of proteins as well as multimeric protein-protein and DNA-protein complexes in near real-time and in buffered solutions. Here, we use tapping-mode AFM to visually analyze the interaction of the essential eukaryotic molecular chaperone protein hsp90 with the glucocorticoid receptor (GR), a well-established hsp90 client protein. An issue of debate within the hsp90 community has been to what extent hsp90 works independently of other molecular chaperones, such as hsp70, or as part of a multiprotein machinery.
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