Related Experiment Video
Updated: Jun 9, 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
Novel helical foldamers: organized heterogeneous backbone folding in 1 : 1 alpha/nucleoside-derived-beta-amino acid
Srivari Chandrasekhar1, Nayani Kiranmai, Marelli Udaya Kiran
1Organic Division-I, Indian Institute of Chemical Technology (CSIR), Uppal Road, Tarnaka, Hyderabad-500 607 (AP), India. srivaric@iict.res.in
Abstract:
Secondary structural conformation of hybrid oligo-peptides comprised of 1 : 1 alternating Nucleoside Derived beta-Amino acid (NDA) and l-amino acid residues has been reported. The studies reveal that the NDA residues organize the heterogeneous backbone featuring the surface properties of both nucleic acids and peptides, to adopt a novel 11/8-helical fold.
Related Concept Videos
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence.
Protein Organization
The primary structure of a protein is its amino acid sequence.
Protein Organization
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

