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

We investigate the fine structure of the sp3 hybridized covalent bondgeometry that governs the tetrahedral architecture around the centralC$_\alpha$ carbon of a protein backbone, and for this we develop newvisualization techniques to analyze high resolution X-ray structures in ProteinData Bank. We observe that there is a correlation between the deformations ofthe ideal tetrahedral symmetry and the local secondary structure of theprotein. We propose a universal coarse grained energy function to describe theensuing side-chain geometry in terms of the C$_\beta$ carbon orientations. Theenergy function can model the side-chain geometry with a sub-atomic precision.As an example we construct the C$_\alpha$-C$_\beta$ structure of HP35 chickenvillin headpiece. We obtain a configuration that deviates less than 0.4 \.A inroot-mean-square distance from the experimental X-ray structure.

On correlation between protein secondary structure, backbone bond angles, and side-chain orientations