English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The original Ramachandran plot is a potent way to understand structures of biomolecules, however only backbone conformations are considered. We formulate a new interpretation of the original Ramachandran plot ( ϕ‐ψ ) that can include a description of the weaker interactions including both the hydrogen bonds and HH bonds as a new way to derive insights into the phenomenon of peptide folding. Specifically, we show that QTAIM analysis permits identifying key regions of the Ramachandran plot without the need for massive data sets. The QTAIM interpreted Ramachandran plot is derived from QTAIM eigenvectors and not a trivial coordinate transformation. An investigation of both the backbone and the weaker bonds within the framework of the QTAIM interpreted Ramachandran plot was found to be in line with physical intuition. The least‐preferred directions calculated for the hydrogen bonds and HH bonds were found to coincide with the “unlikely” regions of the Ramachandran plot.

The role of weak interactions in characterizing peptide folding preferences using a QTAIM interpretation of the Ramachandran plot (ϕ‐ψ)