A survey of a range of proteins that are upregulated during stress and their mechanistic role in causing protein folding diseases

Abstract

Stress is the body's method of reacting to a condition such as a threat, challenge or physical and psychological barrier. According to the World Health Organization, stress has been dubbed the Health Epidemic of the 21st century. Over the past two years, almost three quarters (74%) of people have at some point felt stressed in that they felt overwhelmed, and over half of adults (51%) who felt stressed reported feeling depressed, and 61% reported feeling anxious. This study was aimed to survey a range of proteins that are upregulated in response to stress and their mechanistic role in the development of protein folding diseases. The analysis required the use of different commands and this was done using Jmol, which is a molecular viewer. The structures of proteins upregulated in response to stress were downloaded from the protein data bank. There are nine major eukaryotic proteins upregulated during stress response which included; Heat shock protein 100, Heat shock protein 90, Heat shock protein 70, Heat shock protein 60, Heat shock protein 56, Heat shock protein 47, Heat shock protein 32, Heat shock protein 27 and Ubiquitin. Hsp100, Hsp70, Hsp32 and Ubiquitin had protein molecules containing active sites that bind other molecules. In conclusion, more 3D protein structures of proteins upregulated during stress response are further studied and expressed and deposited in the Protein Data bank so that more of their structural features are further understood and related to function as they play a critical role is preventing protein misfolding.