期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 120, 期 36, 页码 9549-9563出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.6b04886
关键词
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资金
- NSF [1149992]
- RCSA (Cottrell Scholar award)
- Laufer Center
- NIH [R01GM063592-14]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1149992] Funding Source: National Science Foundation
We review how major cell behaviors, such as bacterial growth laws, are derived from the physical chemistry of the cell's proteins. On one hand, cell actions depend on the individual biological functionalities of their many genes and proteins. On the other hand, the common physics among proteins can be as important as the unique biology that distinguishes them. For example, bacterial growth rates depend strongly on temperature. This dependence can be explained by the folding stabilities across a cell's proteome. Such modeling explains how thermophilic and mesophilic organisms differ, and how oxidative damage of highly charged proteins can lead to unfolding and aggregation in aging cells. Cells have characteristic time scales. For example, E. coli can duplicate as fast as 2-3 times per hour. These time scales can be explained by protein dynamics (the rates of synthesis and degradation, folding, and diffusional transport). It rationalizes how bacterial growth is slowed down by added salt. In the same way that the behaviors of inanimate materials can be expressed in terms of the statistical distributions of atoms and molecules, some cell behaviors can be expressed in terms of distributions of protein properties, giving insights into the microscopic basis of growth laws in simple cells.
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