I have been teaching a couple of courses quite regularly since I joined IISER Bhopal. In the odd semester, we offer a course on Structural Biology (403) as part of theBS-MS (Dual Degree) programme.It is also offered to PhD students (623). It is a four-credit course (Three hours of lecture per week), aimed to build the foundation in protein and nucleic acid structure. I begin with the introduction to the hierarchy of protein structure; spend a couple of lectures on refreshing the distance, angle and torsion angle calculations using basic vector algebra. Introduce the students towards the forces that shape up the biomolecules. Myself, I have taken a similar course (Protein confirmation) at MBU, IISc, Bangalore taught by Prof. C Ramakrishnan (CR), one the GN Ramachandran’s students, during my PhD days. The lucid teaching method which CR adapted with a stick representing a chemical bond inspires and makes me improvise real life examples in my lectures. I try to convince students; particularly the ones with immense interest in the sections other than biomolecular structures to at least remember that there exists a rule which says which conformation is right and which one could be wrong.Almost till mid semester exam, I drag on to discuss about various topics on protein structure, like domains (how to define), fold, and Super-secondary structures. I also touch upon the historical triple helix structure of collagen. The students are introduced to some of the practical aspects such as how to compare (superimpose), determine protein-ligand interaction, etc. using freely available software. A few classes are spent discussing conformational flexibility in DNA, and various types of DNA structures. Post mid-semester exam, I focus on the structures of RNA. The course is concluded with discussions on various large macromolecular assemblies such as virus particles, ribosomes, etc. The course requires basic knowledge of biomolecules. I extensively use Swiss PDB viewer during the lectures to demonstrate various 3D aspects. Most of the assignments are worked out using the software. The detailed course content is provided in the curriculum. I mostly follow two textbooks, 1. Protein structures are covered in the book by Schulz and Schirmer called, Principle of protein structures. 2. Nucleic acid structure is followed from the text book on structural biology by Anders Liljas.

For the last few years, I have started taking a course on fundamentals of Biochemistry (Bio 303/603), mostly introducing undergraduate Biology students to the world of biomolecules, their functions, specifically focussing on enzymes and their properties. I tend to follow Voet and Voet as well as Lehninger’s books. For the numerical, Segl’s Biochemical Calculations is the book I followed. There are three conceptual themes on which this course is built, 1. Biomolecular interactions - affinity, rate constants, kinetics of binding etc. 2. Enzyme kinetics including different types of enzyme inhibition, 3. Bioenergetics. I extensively use Swisspdb viewer to discuss structure-function relations in explaining ligand-macromolecule interactions. The classroom teaching for this course also goes in parallel to the laboratory course to introduce the students to assay enzyme activity using Calf Alkaline Phosphatase as a model enzyme.

I have also taught a course on Cell biology for the undergraduate Biology major students (Bio301/Bio601). The textbook by Pollard and Earnshaw and Karp’s Cell biology are the ones I prefer to teach from

During even semester, I have been teaching a course (Bio 302/602)on Biochemistry. The course is again a mandatory course for the 3rd year students enrolled in BS-MS (Dual Degree). In the odd semester, the third-year BS-MS students take a course (Bio 303/03) on Biochemistry which builds a foundation in biochemistry with an introduction to enzyme kinetics, understanding biomolecular interactions and bioenergetics along with initiation of the fundamental metabolic processes, such as Glycolysis and TCA cycle. I begin from TCA cycle as refreshment. I have to confess; as a master's student, this course was the least appealing to me. Therefore, I make a sincere effort to prevent students thinking the same about this course when they reach my stage after 10-15 years. This course is designed to teach various topics in metabolism.

It begins with a very basic understanding on second law of thermodynamics to describe feasibility of a given metabolic process. I mainly focus on teaching concepts in electron transport chain using basic understanding in thermodynamics. A detail description of the system is followed from Voet and Voet. It is followed by fatty acid metabolism, amino acid metabolism and a very organized and brief description of nucleotide metabolism. Few lectures at the end are used to appreciate how these various metabolic processes are coordinated by hormonal activity and energy need in human body. Molecular basis of various human metabolic disorders are discussed briefly at the appropriate times. I mainly follow Principles of Biochemistry by Voet and Voet but also recommend Lehninger as a good read.


Reference :

  • 1. Principles of protein structure by G E Schulz and R H Schirmer (Springer)
  • 2. Text book of structural biology by Anders Liljas (World scientific)
  • 3. Protein structures and molecular properties by Thomas Crighton (W H Freeman)
  • 4. Principles of Biochemistry by Voet and Voet (wiley)
  • 5. Lehninger principles of biochemistry by Nelson and Cox (W H Freeman)
  • 6. Biochemical Calculations by Irwin Segal
  • 7. Karp’s Cell and Molecular Biology, Willey.
  • 8. Cell Biology by Pollard and Earnshaw