Related Experiment Video
Updated: May 20, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 15, 2010
Helical folding in heterogeneous foldamers without inter-residual backbone hydrogen-bonding
Gowri Priya1, Amol S Kotmale, Rupesh L Gawade
1Division of Organic Synthesis, National Chemical Laboratory, Dr Homi Bhabha Road, Pune 411 008, India.
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 Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...

