Related Experiment Video
Updated: Aug 7, 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
Comparison of fully optimized alpha- and 3(10)-helices with extended beta-strands. An ONIOM density functional theory
Robert Wieczorek1, J J Dannenberg
1Department of Chemistry, City University of New York-Hunter College and the Graduate School, 695 Park Avenue, New York, New York 10021, USA.
Abstract:
We compare the structures and energies of beta-strands, alpha-helices, and 3(10)-helices for capped polyalanines, acetyl(ala)(N)()NH(2), for values of N from 2 to 18, using completely optimized mixed DFT/AM1 calculations. Non-pairwise additive cooperativity is manifest from the variation of the relative energies, helical strain, dipole moments, and H-bond lengths of both types of helices, but especially for the alpha-helices. While the gas-phase 3(10)-helices are more stable for small polyalanines, largely due to the additional H-bond, the alpha-helices become relatively more stable as the polyalanines increase in size.
Related Concept Videos
Protein Organization
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Molecular Geometry and Dipole Moments
Protein Organization
The primary structure of a protein is its amino acid sequence.

