Interplay of Intra- and Intermolecular H-Bonding in a Progressively Solvated Macrocyclic Peptide

Abstract

Hydrated in a Hurry Water has a major influence on the conformation of proteins and related biomolecules. However, so many water molecules participate in the hydrogen bonding networks that it can be difficult to pinpoint which specific interactions play the biggest role. Nagornova et al. (p. 320 ) sought to answer this question for the case of a 10–amino acid ring—the antibiotic compound Gramicidin S—by probing the conformational impact of successive additions of one to 50 water molecules to the naked gas-phase structure. The primary changes in the overall ring geometry came from the addition of just the first two waters.