Longer charged amino acids favor β‐strand formation in hairpin peptides

Volume: 27, Issue: 9
Published: Jun 10, 2021
Abstract
Interactions between charged amino acids significantly influence the structure and function of proteins. The encoded charged amino acids Asp, Glu, Arg, and Lys have different number of hydrophobic methylenes linking the backbone to the charged functionality. It remains to be fully understood how does this difference in the number of methylenes affect protein structure stability. Protein secondary structures are the fundamental three-dimensional...
Paper Details
Title
Longer charged amino acids favor β‐strand formation in hairpin peptides
Published Date
Jun 10, 2021
Volume
27
Issue
9
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