Multifaceted folding in a foldamer featuring highly cooperative folds.
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.
Division of Organic Synthesis, National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India.
Veera V E
VV
Ramesh
Gowri
G
Priya
Amol S
AS
Kotmale
Rajesh G
RG
Gonnade
Pattuparambil R
PR
Rajamohanan
Gangadhar J
GJ
Sanjayan
D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D010455:Peptides