Hydrogen bonds shown to play 'conserved' role in protein folding

By changing individual atoms in key places in proteins, Duke University chemists have found new evidence for the importance of comparatively weak "hydrogen bonds" in enabling stringlike proteins to fold into the maximally stable shape they need to assume their roles as biological workhorses. Such protein folding immediately after proteins are synthesized is central to their function in the cell.

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<p><a href="http://www.physorg.com/news10776.html">Hydrogen bonds shown to play 'conserved' role in protein folding</a></p> <p>By changing individual atoms in key places in proteins, Duke University chemists have found new evidence for the importance of comparatively weak "hydrogen bonds" in enabling stringlike proteins to fold into the maximally stable shape they need to assume their roles as biological workhorses. Such protein folding immediately after proteins are synthesized is central to their function in the cell.</p>