(Lecture 3. Instructor: MAI.) This week and next week belong to nuclear magnetic resonance spectroscopy — the technique that reads a molecule’s structure from how its nuclei respond to a magnetic field. It’s taught back to back with the chemistry, method-development, and risk framework from the last two weeks still fresh, and right before atomic spectroscopy picks the small-molecule toolkit back up.
What this session covers
- The physical basis of NMR: nuclear spin, the applied field, resonance.
- ¹H and ¹³C NMR as the two workhorse experiments.
- Chemical shift, coupling, and integration — what each tells you about a structure.
- Problems assigned for next class.
Where this fits in the course
NMR doesn’t get a dedicated technique week later in the term the way atomic and molecular spectroscopy do, but it shows up as a working tool elsewhere: solid-state NMR appears in Week 6’s polymorph toolbox, 2D-NMR is one of the higher-order-structure methods for a biologic, and ¹H NMR is the technique that caught the heparin/OSCS adulteration case discussed later in the term. This week and next give you the fundamentals those later mentions assume.
Source note. (Instructor MAI: this page is a scheduling placeholder — replace with your own material and problem set.)