Backbone Hydration of <i>α</i>-Helical Peptides: Hydrogen-Bonding and Surface Hydrophobicity/Hydrophilicity.

ABSTRACT: The stability of proteins and small peptides depends on the way they interact with the surrounding water molecules. For small peptides, such as α-helical polyalanine (polyALA), water molecules can weaken the intramolecular hydrogen-bonds (HB) formed between the peptide backbone O and NH groups which are responsible for the α-helix structure. Here, we perform molecular dynamics simulations to study the hydration of polyALA, polyserine (polySER), and other homopolymer peptide α-helices at different temperatures and pressures. We find that water molecules form HB with most polyALA carbonyl O atoms, despite ALA hydrophobic CH₃ side chain. Similar water-peptide backbone HB are found in other (hydrophobic and hydrophilic) homopolymer α-helices with large si

SUBMITTER: Eltareb A 

PROVIDER: S-EPMC11753776 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature