Journal
BIOESSAYS
Volume 32, Issue 8, Pages 655-658Publisher
JOHN WILEY & SONS INC
DOI: 10.1002/bies.201000038
Keywords
fitness; mutation; protein folding; split beta-lactamase assay; stability-function tradeoff
Categories
Funding
- National Science Foundation [MCB-0749836]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0749836] Funding Source: National Science Foundation
Ask authors/readers for more resources
A new split beta-lactamase assay promises experimental testing of the interplay of protein stability and function. Proteins are sufficiently stable to act effectively within cells. However, mutations generally destabilize structure, with effects on free energy that are comparable to the free energy of folding. Assays of protein functionality and stability in vivo enable a quick study of factors that influence these properties in response to targeted mutations. These assays can help molecular engineering but can also be used to target important questions, including why most proteins are marginally stable, how mutations alter structural makeup, and how thermodynamics, function, and environment shape molecular change. Processes of self-organization and natural selection are determinants of stability and function. Non-equilibrium thermodynamics provides crucial concepts, e.g., cells as emergent energy-dissipating entities that do work and build their own parts, and a framework to study the sculpting role of evolution at different scales.
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