Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 35, Pages 9209-9212Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201403784
Keywords
gas-phase structures; mass spectrometry; protein folding; protein structures
Categories
Funding
- American Society for Mass Spectrometry
- Oak Ridge Associated Universities
- National Science Foundation (CAREER Award) [1253384]
- Direct For Mathematical & Physical Scien [1253384] Funding Source: National Science Foundation
- Division Of Chemistry [1253384] Funding Source: National Science Foundation
Ask authors/readers for more resources
The three-dimensional structures adopted by proteins are predicated by their many biological functions. Mass spectrometry has played a rapidly expanding role in protein structure discovery, enabling the generation of models for both proteins and their higher-order assemblies. While important coursed-grained insights have been generated, relatively few examples exist where mass spectrometry has been successfully applied to the characterization of protein tertiary structure. Here, we demonstrate that gas-phase unfolding can be used to determine the number of autonomously folded domains within monomeric proteins. Our ion mobility-mass spectrometry data highlight a strong, positive correlation between the number of protein unfolding transitions observed in the gas phase and the number of known domains within a group of sixteen proteins ranging from 8-78 kDa. This correlation and its potential uses for structural biology is discussed.
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