Folding of Protein Ions in the Gas Phase after Cation-to-Anion Proton-Transfer Reactions.

ABSTRACT: The structure and folding of a protein in solution depends on noncovalent interactions within the protein and those with surrounding ions and molecules. Decoupling these interactions in solution is challenging, which has hindered the development of accurate physics-based models for structure prediction. Investigations of proteins in the gas phase can be used to selectively decouple factors affecting the structures of proteins. Here, we use cation-to-anion proton-transfer reactions (CAPTR) to reduce the charge states of denatured ubiquitin ions in the gas phase, and ion mobility to probe their structures. In CAPTR, a precursor charge state is selected (P) and reacted with monoanions to generate charge-reduced product ions (C). Following each CAPTR event, denatured ubiquitin ions (13+ to 6+)

SUBMITTER: Laszlo KJ 

PROVIDER: S-EPMC4999245 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature