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Updated: Jul 1, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Arginine zwitterion is more stable than the canonical form when solvated by a water molecule
Suk Im1, Sung-Woo Jang, Sungyul Lee
1College of Environmental Science and Applied Chemistry (BK21), Kyunghee University, Kyungki 449-701, S. Korea.
Abstract:
We present calculations for the Arg-H2O system and predict that the zwitterionic Arg is thermodynamically more stable than the canonical form in the gas phase under the influence of a single water molecule because of the strongly basic guanidine side chain. Canonical conformers of Arg-H2O are found to isomerize to the zwitterionic forms via a small barrier (approximately 6 kcal/mol).
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