Course Identification

NMR of proteins

Lecturers and Teaching Assistants

Prof. Jacob Anglister, Dr. Tali Scherf, Dr. Rina Rosenzweig
Dr. Or Szekely

Course Schedule and Location

Second Semester
Monday, 14:15 - 16:00, Kimmelman, Dov Elad Rm

Tuesday, 11:15 - 12:00, Perlman, Rm 404

Field of Study, Course Type and Credit Points

Chemical Sciences: Lecture; Elective; 2.00 points
Life Sciences: Lecture; Elective; 2.00 points







Language of Instruction


Attendance and participation

Expected and Recommended

Grade Type

Numerical (out of 100)

Grade Breakdown (in %)


Evaluation Type

Final assignment

Scheduled date 1

The final assignment for the course will consist of 2 parts: a seminar and a written assignment.
As part of the final evaluation, the students are required to critically read and evaluate two NMR papers. One should be presented during a class seminar (12 min seminar + 8 min Q&A session) and the second
paper should be submitted as a written assignment (up to 4 pages in length).
Will take place on July 26th and August 2nd, 09:00-13:00, at FGS room A.

Estimated Weekly Independent Workload (in hours)



This course is given for Chemistry and Life Sciences Students. The aim of the course is to give an overview of the application of NMR for determining the three dimensional structure of proteins and for studying protein-ligand and protein-protein interactions. Topics to be covered: Basic principles of NMR (short introduction), two dimensional NMR techniques, sequential assignment of peptides and proteins, determination of the secondary structure of proteins, use of 3D and 4D NMR for larger proteins, structure calculation, transferred NOE and other techniques for studying protein/ligand interactions, hydrogen exchange techniques and their application for studying protein folding and most recent advanced NMR methodologies for studying protein structure.

Learning Outcomes

Upon successful completion of this course students should be able to:

  1. Critically read and review current literature which describes the use of NMR for structural studies of proteins and their interactions with ligands.
  2. Understand the capabilities and limitations of NMR in studying the structure of proteins in solution and its advantages and disadvantages over X-ray crystallography.

Reading List

  1. Kurt Wuthrich, NMR of Protein and Nucleic Acids
  2. G.C.K. Roberts NMR of Macromolecules, A Practical Approach
  3. An NMR Primer for Life Scientists
  4. Jeremy N. S. Evans, Biomolecular NMR Spectroscopy
  5. Protein NMR Techniques, Methods in Molecular Biology Vol 60 1997 edited by David G. Reid