title: A direct comparison of protein structure in the gas and solution phase: the Trp-cage.
abstract: Molecular dynamics simulations of zwitterions of the Trp-cage protein in the gas phase show that the most stable ion in vacuo has preserved the charge locations acquired in solution. A direct comparison of the gas and solution-phase structures reveals that, despite the similarity in charge location, there is significant difference in the structures, with a substantial increase in hydrogen bonds and exposure of hydrophobic parts in the gas phase. The structure of the salt bridge in the gas phase is also much more stable than in the (experimental) solution structure.
authors.forename: Alexandra
authors.initials: A
authors.lastname: Patriksson
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Adams
authors.forename: Frank
authors.initials: F
authors.lastname: Kjeldsen
authors.forename: Roman A
authors.initials: RA
authors.lastname: Zubarev
authors.forename: David
authors.initials: D
authors.lastname: van der Spoel
mesh_terms: D005740:Gases / Q000737:chemistry; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions
chemical_list: D005740:Gases; D010455:Peptides; D012996:Solutions; C508725:Trp-cage peptide