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Fast folding for synthetic peptides and microproteins

Researchers at Xi'an Jiaotong-Liverpool University developed a new method that enables the efficient production of cysteine-rich peptides and microproteins in their naturally folded 3D structure. The approach uses organic solvents to mimic nature's oxidative folding process, resulting in speeds of over 100,000 times faster than aqueous...

SourceXi'an Jiaotong-Liverpool University·JournalAngewandte Chemie·TypeExperimental study·DateMar 21, 2024

Biophysicists manipulate 'zipper,' reveal protein folding dynamics

Researchers at TUM have successfully manipulated a single 'zipper' protein molecule to map changes in its energy landscape during folding and unfolding. This breakthrough provides higher-resolution measurements of protein folding dynamics, shedding light on the chain of events leading from DNA coding to biological function.

SourceTechnical University of Munich (TUM)·JournalProceedings of the National Academy of Sciences·DateJan 18, 2010