title: Proteins with highly similar native folds can show vastly dissimilar folding behavior when desolvated.
abstract: Proteins can be exposed to vastly different environments such as the cytosol or membranes, but the delicate balance between external factors and intrinsic determinants of protein structure, stability, and folding is only poorly understood. Here we used electron capture dissociation to study horse and tuna heart Cytochromes c in the complete absence of solvent. The significantly different stability of their highly similar native folds after transfer into the gas phase, and their strikingly different folding behavior in the gas phase, can be rationalized on the basis of electrostatic interactions such as salt bridges. In the absence of hydrophobic bonding, protein folding is far slower and more complex than in solution.
authors.affiliation: Institut für Organische Chemie and Center for Molecular Biosciences Innsbruck (CMBI), Universität Innsbruck, Innrain 80-82, 6020 Innsbruck (Austria) http://www.bioms-breuker.at.
authors.forename: Moritz
authors.initials: M
authors.lastname: Schennach
authors.forename: Kathrin
authors.initials: K
authors.lastname: Breuker
mesh_terms: D000596:Amino Acids; D000818:Animals; D005740:Gases / Q000737:chemistry*; D006736:Horses; D013058:Mass Spectrometry; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D005740:Gases; D011506:Proteins
keywords: electron capture dissociation; gas phase; mass spectrometry; protein; protein folding