Journal
STRUCTURE
Volume 22, Issue 4, Pages 572-581Publisher
CELL PRESS
DOI: 10.1016/j.str.2014.02.001
Keywords
-
Funding
- New Faculty Award from the Camille & Henry Dreyfus Foundation
- National Science Foundation [MCB-0845033]
- National Institutes of Health [R01-GM086507, R01-GM101135]
- American Cancer Society [RSG-12-161-01-DMC]
- Research Corporation for Science Advancement
- Northeastern University Office of the Provost
- European Social Fund under the Global Grant measure
- Waters Corporation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0845033] Funding Source: National Science Foundation
Ask authors/readers for more resources
The relationship between protein sequence, structure, and dynamics has been elusive. Here, we report a comprehensive analysis using an in-solution experimental approach to study how the conservation of tertiary structure correlates with protein dynamics. Hydrogen exchange measurements of eight processivity clamp proteins from different species revealed that, despite highly similar three-dimensional structures, clamp proteins display a wide range of dynamic behavior. Differences were apparent both for structurally similar domains within proteins and for corresponding domains of different proteins. Several of the clamps contained regions that underwent local unfolding with different half-lives. We also observed a conserved pattern of alternating dynamics of the a helices lining the inner pore of the clamps as well as a correlation between dynamics and the number of salt bridges in these a helices. Our observations reveal that tertiary structure and dynamics are not directly correlated and that primary structure plays an important role in dynamics.
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