Analysis of the Properties of Protein that Require Chaperones
The protein folding problem is one of the largest problems facing biologist today. Many diseases are caused by protein aggregation and or misfolding of proteins. Understanding how polypeptide chains fold to obtain their native conformational state as a functional protein is vital to making the link between the structure and the function of proteins. Being able to predict the structure and function of a protein from it's amino acid sequence will one day allow us to manufacture protein with specific functions, the ability to cure certain diseases will be one of the many benefits. Most proteins after translation are able to fold independently into their native conformational states others require the help of molecular chaperones. I will be studying a set of proteins that require molecular chaperones to fold. Using online resources such as the Medline and the Protein Data Bank (PDB). I will create a study sample of 50 proteins with known structures that require chaperones to fold properly. I will develop a classification scheme elucidating the different types of chaperone action utilized to assist in the folding of these proteins. I will catalogue these proteins and classify their structures, obtained from the PDB, using the above mentioned scheme and present these results on a web page. I will then analyze physical /structural properties of the study sample to establish weather or not patterns exist that would correlate them to specific classes of chaperone action and or classes of proteins which do not require chaperones. The goal of this research is to elucidate whether the protein folding problem is unique for proteins that require chaperones.
