<h3>Title</h3>
<h3>Design and Engineering of Natural and Artificial Biocatalyst using Directed Evolution and De novo Design Approaches for Sustainable Chemistry</h3>
<p><strong><span style="text-decoration: underline;">Abstract</span> :</strong></p>
<p>Proteins are molecular machines whose function depends on their ability to achieve complex folds with precisely defined structural and dynamic properties. AlphaFold, Rosetta, and machine learning approaches have been a breakthrough in the field of protein design and structure determination which can be used to predict quite accurately the secondary structure of most proteins from many different families. However, to achieve an “active” or “attractive” protein/enzyme is still a challenging feat which can be tackled using protein engineering. Continuing from my talk yesterday, I will describe how purposeful introduction of mutation can be beneficial for improving properties of a protein using examples of Cytochrome P450 and an artificial dirhodium cyclopropanase. Furthermore, I will describe “de novo protein design approach”, a rational way of designing proteins from scratch based on principles of protein folding, thermodynamics, and energetics using an exemplar of a four-helix bundle and a heme metal co-factor. Concluding my talk will be a roadmap to future research directions based on a) metalloenzymes for green chemistry and sustainable catalysis and b) study of metalloproteins as sensors in redox cellular pathways, imbalances in which are associated with a variety of diseases (cancer, neurological disorders, tuberculosis) using<br />mutagenic, metal-substitution, and protein engineering approaches.</p>