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 Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

A 20 x 20 table of tripeptides has been compiled that may be used to locate beta-sheet breaking and alpha-helix breaking residues in proteins. It is based on the definition of an alpha-helical and a beta-sheet domain on the (varphi, Psi) map based on the occurrences of alpha-helices and beta-sheets in 12 known proteins whose sequence and three-dimensional structure have been determined. Each entry in the 20 x 20 table lists three numbers, the frequency of occurrences of the middle amino acid (n) in relation to its nearest neighbors (n - 1) and (n + 1) in the alpha-helical domain, the beta-sheet domain and outside these regions. The regions between two beta-sheet-breaking residues would be permissively beta-sheet regions. The sequence of concanavalin A has been examined in this manner and of the 13 beta-strands defined by x-ray crystallography, 10 were in agreement with the permissively beta-sheet regions and, in the remaining three, beta-sheet-breaking residues were the third in one, and the third, fourth, and fifth residues in another, and the sixth residue in the third from the beginning of the beta-strands. The findings provide strong support for the role of nearest-neighboring amino acids in determining secondary structure of proteins.

proceedings of the national academy of sciences of the united states of america

The Influence of Nearest-Neighbor Amino Acids on the Conformation of the Middle Amino Acid in Proteins: Comparison of Predicted and Experimental Determination of β-Sheets in Concanavalin A