Funding was provided by the Austrian Science Fund (FWF): Y372 to K.B.
Proteins with Highly Similar Native Folds Can Show Vastly Dissimilar Folding Behavior When Desolvated†
Article first published online: 20 NOV 2013
© 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.
Volume 126, Issue 1, pages 168–172, January 3, 2014
How to Cite
Schennach, M. and Breuker, K. (2014), Proteins with Highly Similar Native Folds Can Show Vastly Dissimilar Folding Behavior When Desolvated. Angew. Chem., 126: 168–172. doi: 10.1002/ange.201306838
- Issue published online: 23 DEC 2013
- Article first published online: 20 NOV 2013
- Manuscript Revised: 7 OCT 2013
- Manuscript Received: 5 AUG 2013
- Funded Access
- Austrian Science Fund (FWF). Grant Number: Y372
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.