Direct observation of Hsp90-induced compaction in a protein chain

The chaperone heat shock protein 90 (Hsp90) is well known to undergo important conformational changes, which depend on nucleotide and substrate interactions. Conversely, how the conformations of its unstable and disordered substrates are affected by Hsp90 is difficult to address experimentally yet is central to its function. Here, using...

Visualising Conformational Changes in HSP90 Protein using Plasmonic Nanoapertures

In this thesis, we demonstrate optical trapping of HSP90 proteins in plasmonic nanoapertures to study the HSP90 conformational change. This technique is label-free and non-destructive. The resonance of the bow tie shaped plasmonic nanoaperture is used to create a very strong electric field gradient force able to trap proteins. The resonance...