PUBLICATION HIGHLIGHT
Why do proteins fold?
This publication highlight is part of the SBGrid/Meharry Medical College Communities Project, focused on science education and demonstrating how structural biology and preclinical science connect to medicine.
Proteins are the movers and actors of the cell. These molecular machines are responsible for carrying out the functions necessary for life’s survival, like building and destroying compounds, moving ions across the membrane, and sensing changes in the environment. The ability of proteins to carry out this wide array of functions is dependent on their ability to form unique and purposeful shapes. The structure of the proteins is what determines its function. But, some proteins carry out highly specific, highly vital functions without folding into any consistent structure. Understanding how and why proteins fold into these complex structures or decide not to fold at all is still an open topic of investigation. Specifically, understanding what factors affect protein folding and shape could provide insight into the underlying mechanism. In a recent study in Protein Science, SBGrid member Dr. Tobin Sosnick from The University of Chicago, provides observations on forces that influence protein stability in a wide range of different environmental conditions.
Using solution based structural methods and simulation, Dr. Sosnick observed how unstructured proteins respond to temperature and ion concentration. These findings showed that the shape of these unstructured proteins were dependent on both ion concentration of buffer and temperature. Using a clever experimental design, he and his team were able to show that while the well researched hydrophobic effect was a major contributor to protein stabilized shapes, other forces also influence protein stability. Forces like hydrogen bonding and van der Waal packing were shown to influence the size and shape of these disordered proteins in solution. This article provides interesting observations into the concert of forces at play in the macromolecular world and generates interesting questions about how environmental cues can select for structural modifications.
Read more in Protein Science.
By Vida Robertson, Fisk University
Vida Storm Robertson is a Masters Student in Chemistry at Fisk University working in both solid-state and solution based structural determination techniques. He will begin his PhD in Biochemistry and Molecular Biophysics at Caltech this summer.
