# Forces behind N- and C-capping of peptidic helices

## TL;DR

This paper investigates how N- and C-capping motifs stabilize helical peptides differently, focusing on their effects on structure and stability.

## Contribution

The study compares N- and C-capping motifs in peptides, revealing distinct impacts on helix stability and folding.

## Key findings

- N-capped helices exhibit more rigid helical structures.
- C-capped helices show greater unwinding entropy.

## Abstract

Helical peptides are primarily stabilized by intramolecular hydrogen bonds. Particular conformational arrangements, capping motifs, help precisely terminate helices by compensating for disruption of helical H-bonding patterns. This contribution explores if: (i) N-and C-caps are essentially the same; and, (ii) how differences impact their thermodynamic helix stabilities and folding kinetics.

Helicity is more rigidly imposed in the N-capped system, and unwinding entropy is greater for the C-capped one.