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. Electron capture dissociation has been used to study horse (example at the top) and tuna (example at the bottom) heart cytochromes c in the complete absence of solvent. It was shown that in the absence of hydrophobic bonding, folding is slow, complex, and driven by electrostatic interactions. Y=Yield. © 2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.