Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 4, Pages 1177-1180Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja308528d
Keywords
-
Categories
Funding
- German Academy of Sciences Leopoldina
Ask authors/readers for more resources
There is ongoing debate about the extent to which protein structure is retained after transfer into the gas phase. Here, using ion-mobility spectrometry, we investigated the impact of side-chain backbone interactions on the structure of gas-phase protein ions by noncovalent attachment of crown ethers (CEs). Our results indicate that in the absence of solvent, secondary interactions between charged lysine side chains and backbone carbonyls can significantly influence the structure of a protein. Once the charged residues are capped with CEs, certain charge states of the protein are found to undergo significant structural compaction.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available