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perceived in two ways: 1) Some proteins are having the “bad boy” persona, 2) For some external factors impact their functional activity, it’s like transforming good boy into bad boy. This reminds me of my mother’s warnings “Don’t play with this boy, he might make you unlearn your good habits.” So how does this happen? To understand this we should know how proteins are formed? Biologically, proteins exist in a linear chain of amino acids (also called “polypeptide chain”) and it’s known as the primary structure of proteins. To acquire functionalproperties,proteinstartsfoldingand it gains secondary, tertiary and quaternary structure and the final state is called the native conformation. Protein folding is just like a developing baby in a mother’s womb and during this folding process if some problem occurs (“misfolding”), it loses its native conformation and resulting in neurological diseases (for example, Alzheimer’s and Parkinson’s) and hence, protein
portrays itself as a bad boy.
In another case, a protein is
affected by another protein,
which creates a negative
coalition and leads to disease
and, hence, a single, free-
flowing, innocent protein when it
interacts with bad, dirty and evil
protein it causes diseases like
cancer, bacterial infections and neurodegenerative disease. So
overall, it is proteins that have
troubled your grandmother with
knee pain (Rheumatoid Arthritis),or forcing your parents to take insulin injections to control their diabetes, and making people die of cancer. Since then, the whole scientific community is continuously putting their efforts to control these bad boys by designing drug molecules against them to stop their unwanted/abnormal functional activities.
Protein structure-dynamic study has
Mr. Mitul Srivastava || 241
always captured the attention of the scientific community because of their complex nature, different shapes and sizes and, in return, it has given us many Nobel laureates, like Sir Robert J. Lefkowitz, Sir Brian K. Kobilka (2012), and Sir Richard Henderson (2107). Protein entered in my body system when I was growing up and I entered into the protein world during my post- graduation by choosing bioinformatics and, more specifically, structural bioinformatics as a subject for my major, to understand protein functions in the body system. As a structural bioinformatician, I am passionate about Homology Modeling (building protein models), Molecular Docking (protein-ligand association), Molecular Dynamics (assimilating protein dynamic nature) and, overall, Computer-aided Drug Designing. The whole world of proteins their structure, functions and biological mechanism fascinated me so much that I decided to continue with this subject
in for my Ph.D.. Along with proteins, cancer, which is full of complexities and challenges also compelled me to choose it as my disease model in my thesis work.
I started working on Ubiquitin Proteasome System (UPS), which is a parallel mechanism like Autophagy for degradation of proteins. UPS has several components that work together to degrade proteins, these are: E1-
activating enzyme, E2-conjugating enzyme, E3-ligases, USPs (Ubiquitin Specific Proteases) and Ubiquitin. In all these components, USPs are major drug targets that are highlighted in different studies and their role in cancers is well documented. USPs are De-ubiquitinating enzymes that are responsible for cleaving ubiquitin from protein that are destined for degradation. The “to be degraded” proteins get
Proteins are the building blocks of human body” and then would come the next tricky question, “How much of your muscle
is composed of proteins” and again we would answered, “80% Ma’am/Sir”