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 structure of (S)-N,N′-di-tert-butyl-2-[N-(1-phenylethyl)benzamido] malonamide contains two fragments of a polypeptide chain. This compound therefore can be taken as a model substance for details of protein conformation. In the crystalline state one peptide chain of the model molecule incorporates a hydrogen bond between two adjacent nitrogen atoms in the backbone. The acceptor for the hydrogen is the p z -orbital at the proton accepting nitrogen. The occurence of such hydrogen bonds in proteins might explain some correlations found between φ and ψ torsion angles. In addition a correlation between torsion angle ψ and the bond angle τ at C α  in the backbone of polypeptide chains could be established. The model substance also contains a “frozen” back side attack of a C = O group on the tetrahedrally coordinated C α  in analogy to the S N 2 substitution reaction of the Walden inversion with a trigonal bipyramidal transition state.

Some Aspects Concerning Conformation of Polypeptide Chains in Proteins