We have discovered that disulfide bonds act as power switches for protein folding. Disulfide bonded titin domains can deliver thousands of zW of mechanical power. See our recent paper on this topic just published in Cell Reports
We have built a novel magnetic tweezers design that allows us to apply an arbitrary force signal to single proteins with a bandwidth of~20 kHz. Our recordings are obtained using a custom C++/Qt program that clocks up to 1700 fps. The results that we obtain are spectacular.
We have designed small peptides that block the formation of isopeptide bonds in the pili of Gram positive pathogens. We demonstrate that blocking isopeptide bonds in pili, weakens them mechanically. Our aim is to perfect these peptides so that they can be used as antibiotics where intervened pili become easy prey for proteases, losing their grip on the host.
What we now know about titin folding should be sufficient to trigger a paradigm shift in our understanding of muscle contraction.