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Updated: May 17, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Multifaceted folding in a foldamer featuring highly cooperative folds
Veera V E Ramesh1, Gowri Priya, Amol S Kotmale
1Division of Organic Synthesis, National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India.
Abstract:
Herein, we report on the folding pattern observed in a synthetic peptide featuring two highly mutually dependent, yet strikingly dissimilar, closed networks of hydrogen-bonded rings that work in a cumulative fashion to stabilize the entire folded architecture of the peptide. Structural studies unequivocally suggest that disruption of any one of these mutually-dependent hydrogen-bonded networks is deleterious to the stability of the fully folded conformation of the peptide.
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