Details

Autor(en) / Beteiligte

• Moon, C. Preston
• Fleming, Karen G.

Titel

Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers

Ist Teil von

• Proceedings of the National Academy of Sciences - PNAS, 2011-06, Vol.108 (25), p.10174-10177

Ort / Verlag

United States: National Academy of Sciences Issue

Erscheinungsjahr

2011

Quelle

MEDLINE

Beschreibungen/Notizen

• The transfer free energies of the twenty natural amino acid side chains from water to phospholipid bilayers make a major contribution to the assembly and function of membrane proteins. Measurements of those transfer free energies will facilitate the identification of membrane protein sequences and aid in the understanding of how proteins interact with membranes during key biological events. We report the first water-to-bilayer transfer free energy scale (i.e., a "hydrophobicity scale") for the twenty natural amino acid side chains measured in the context of a native transmembrane protein and a phospholipid bilayer. Our measurements reveal parity for apolar side-chain contributions between soluble and membrane proteins and further demonstrate that an arginine side-chain placed near the middle of a lipid bilayer is accommodated with much less energetic cost than predicted by molecular dynamics simulations.