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Award ID contains: 2317111

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  1. Understanding how substrate structure alters an enzyme's conformational landscape is central to catalyst design. Using single-molecule electronic sensors, we reveal how substitutions on an HDAC8 substrate modulate the enzyme's underlying catalytic dynamics. We demonstrate that a trifluoroacetyl group accelerates catalysis, while a Boc cap and an allosteric activator synergistically simplify the kinetic pathway by stabilizing productive conformations. These findings provide direct, real-time insight into how substrate-induced conformational dynamics control enzyme catalysis. 
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    Free, publicly-accessible full text available December 9, 2026
  2. Free, publicly-accessible full text available May 19, 2026
  3. A synthetic biomolecular condensate (sBC) was developed using zein, a hydrophobic protein derived from plants. These particles can be used as an artifiical platform to understand the structure and function of natural protein-rich condensates. 
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  4. Self-assembled materials capable of modulating their assembly properties in response to specific enzymes play a pivotal role in advancing 'intelligent' encapsulation platforms for biotechnological applications. Here, we introduce a previously... 
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