Protein sequence encodes complex network of interactions and it is difficult to decipher simple rules in protein science. In spite of this challenge, approximate and semi-empirical rules can be found to describe biophysical properties of different proteins. Using statistical mechanical models tested against multitude of data, our goal is to unravel such universal features of proteins. Our next goal is to extend these transferrable laws in a high throughput manner to model the entire collection of proteins inside an organism, called the proteome. The application at the proteome level allows us to bridge the gap between molecular biophysics and cellular physics and provides us evolutionary insights. With this approach we will try to address some questions of broad interest: i) Why are cells so sensitive to temperature? ii) How do thermophilic proteins (derived from organisms that thrive at high temperature) withstand high temperatures compared to their mesophilic (organisms that live at room temperature) counterparts? iii) What is the evolutionary implication of distribution of different rate processes in a cell and how are they optimized? iv) How do salts slow down cell growth?