A closer look at Type I left-handed β-helices provides a better understanding in their sequence-structure relationship: towards their rational design

Abstract

Understanding the sequence-structure relationship in protein is of fundamental interest, but has practical applications such as the rational design of peptides and proteins. This relationship in the Type I left-handed {beta}-helix containing proteins is updated and revisited in this study. Analysing the available structures in the Protein Data Base, we could describe further in details the structural features that are important for the stability of this fold, as well as its nucleation and termination. This study is meant to complete previous work, as it provides a separate analysis of the N-terminal and C-terminal rungs of the helix. Particular sequence motifs of these rungs are described along with the structural element they form.