Helical folding in heterogeneous foldamers without inter-residual backbone hydrogen-bonding
Chemical Communications2012Vol. 48(71), pp. 8922–8922
Citations Over TimeTop 20% of 2012 papers
G. Priya, Amol S. Kotmale, Rupesh L. Gawade, Deepti Mishra, Sourav Pal, V.G. Puranik, Pattuparambil R. Rajamohanan, Gangadhar J. Sanjayan
Abstract
This communication describes a set of hybrid foldamers that do not feature inter-residual, but intra-residual backbone hydrogen-bonding, yet adopt a preferentially folded conformation displaying right-handed helical architecture. Conformational ordering is apparently due to the combined conformational restrictions imposed by the conformationally restricted individual amino acid residues with which the oligomers are made of.
Related Papers
- → Improving folding properties of computationally designed proteins(2019)8 cited
- → Reshaping the Protein Folding Pathway by Osmolyte via its Effects on the Folding Intermediates(2015)10 cited
- → Comparing the Folding and Misfolding Energy Landscapes of Phosphoglycerate Kinase(2012)7 cited
- → Crystal Structures and Hydrogen Bonding in One-Dimensional Chains of 4,5-Dicyanoimidazole and 4,5-Dichloroimidazole(1995)12 cited
- Prediction of Protein Folding-rate Based on the Residues Contact Number(2013)