Curriculum & Course Descriptions


BS3011 Protein folding & biomolecular NMR

Course Coordinator: Associate Professor Surajit BHATTACHARYYA (email:

Academic Unit: 3 AU

Availability: Semester 2

Pre-requisite: BS2004

Course Type: BS-Major-PE, BMS-Major-PE

Language of instruction: English

Teaching hours: Lectures: 26 hours; Tutorials: 13 hours

Learning Objective: To learn mechanisms of protein folding and applications of NMR in biological systems. To build further analytical skills to solve more sophisticated biophysical and structural biology problems related to drug discovery.

Content: This course introduces protein folding and biomolecular NMR at a more advanced level.

  • Concepts of NMR spectroscopy and protein folding and structure
  • Description of NMR parameters
  • Analyses and interpretations of multidimensional NMR spectra
  • Determination of atomic resolution structures of biomolecules and inter-molecular interactions .
  • Experimental and computational analyses of protein folding processes in vitro and in vivo

Learning Outcome: Students will (i) analyze complex multi-dimensional NMR spectra of biomolecules; (ii) determine atomic resolution structures of proteins and complexes in solution from NMR data, (iii) interpret NMR parameters of protein-protein and protein-ligand interactions; (iv) explain experimental and computational approaches in protein folding mechanisms. With that students are able to establish a solid understanding on applications of bio-NMR and protein folding mechanisms and gain awareness of current research topics.


  • NMR of proteins and nucleic acids: K. Wuthrich
  • Protein NMR spectroscopy: Cavanagh & others
  • Modern NMR techniques for chemistry research: A. Derome
  • Protein folding: T. Creighton
  • Mechanisms of protein folding: R. H. Pain.

*Prerequisites for Incoming Exchange Students: Equivalent of Year 2 or Higher Biology or Biotechnology Major