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For , the thrill of research comes from standing on the precipice of the unknown.

“There is nothing quite like the feeling of striking gold and getting a new piece of critical data,” he said. “At that very moment, you’re likely the only person in the entire world that knows that biology.”

John Melchior refined a technique to separate high-density lipoprotein particles based on the presence of certain proteins.

Melchior researches the structural complexity of high density lipoproteins, or HDL, as a postdoctoral fellow in lab at the . Based on his work, he was selected by the to speak in a special session highlighting up-and-coming researchers at the ¾ÅÓÎÌåÓý annual meeting.

Melchior said he “fell in love with lipoproteins” during his graduate studies at Wake Forest University, where he was trained in lipid biochemistry. He has continued to study lipoproteins, this time from the protein side. He refined a technique to separate HDL particles based on whether they contain a protein called apoA-II and determined that apoA-II is critical for the positive effects of HDL.

“I found this extremely exciting,” he said. “The logical next steps were to understand the role of apoA-II’s structure in modulating this function.”

His initial attempts to understand the structure of apoA-II were halted when that a previously published crystal structure of the protein was falsified. But Melchior sees what he called an “unfortunate setback” as an opportunity for his structural studies to help fill the gaps of what remains unknown about apoA-II.

Melchior hopes his work will benefit the HDL research community as a whole; for him, this community is almost as important as the research itself.

“I’ve been fortunate to establish relationships with some amazing people who also happen to be excellent scientists,” he said. “I’m really grateful for the community and the friendships that have enriched my life.”