Proteins: molecules defined by their trade-offs

Abstract

Proteins are subject to various conflicting forces that trade-off against each other. For example, during folding, the protein achieves lower enthalpy at the cost of lower entropy. Similarly, the trade-off for increased stability may be decreased flexibility, which may abolish allosteric pathways. Accordingly, stability trades-off against function, which may also trade-off against folding kinetics and mechanism. Furthermore, attaining increased stability may reduce a protein's ability to adopt novel functions. Understanding the biophysics and function of proteins requires quantification of the driving forces involved in each of the trade-offs. Indeed, quantification of the linkages in the network of trade-offs is essential to obtaining a more complete understanding of protein structure and function.