Botulinum NeuroToxin (BoNT)

Nick DeNunzio, Rob MacDonald

The neurotoxin produced by the soil-dwelling bacterium Clostridium botulinum is among the most potent toxins known. The toxin is a zinc-dependent endoprotease that disrupts vesicle trafficking at the neuromuscular synapses, effectively blocking neurotransmitter release and leading to the characteristic flaccid paralysis of botulism.
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Haloalkanoic acid dehalogenase superfamily (hadsf)

Kelly Daughtry, Bill Lu, Andrew Lynch, Chetanya Pandya, Dan Saltzberg

The haloalkanoic acid dehalogenase superfamily(HADSF) consists of more than 3000 members in organisms ranging from prokaryotes to humans. Although the superfamily was named after the first family member structurally characterized, 2-haloacid dehalogenase, the vast majority of known catalytic activities carried out by family members are directed at phosphoryl transfer.
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Hotdog fold thioesterase

Lorenzo Finci, Rui Wu

The Hotdog fold, is a domain which is found in eukaryotes, bacteria, and archaea. This domain is involved in many cellular processes, which range from thiester hydrolysis, transcriptional regulation of fatty acid biosynthesis, polychlorinated biphenyls (PCB) degradation, antibiotic biosynthesis, to the degradation of aromatic compounds such as phenylacetic acid.
For more on Hotdog Fold Thioesterases, click here.

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Lanthanide binding tag (lbt)

Kelly Daughtry, Nick DeNunzio, Nikhil Shah

Lanthanide binding tags (LBTs) are the next generation of fluorescent tags. Since this one tag can potentially aid in protein purification, characterization, and structure determination, it could be a very important tool for proteomics research. A newer tag utilizes double-lanthanide-binding tags (dLBT), two short sequences of amino acids (15-25) that selectively bind two lanthanide ions, to assist in protein tagging.
For more on LBTs, click here.

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