Methods for Protein Structure Determination

BCHM 669A: Special Topics, Fall 2006

Course meets in CBSO 2118, Mo(We)Fr 10:00-11:15 am

Professor: David Fushman
Office: Room 1121 Agriculture/Life Sciences Surge Bldg


This graduate level course is designed as an introduction to modern methods for biomolecular structure determination at the atomic level resolution. The course will cover the theory and basic principles underlying of the two major high-resolution experimental methods: X-ray crystallography and nuclear magnetic resonance (NMR). We will also discuss low-resolution experimental methods and theoretical approaches to protein structure prediction and protein molecular dynamics simulations. The course will start with a review of physico-chemical properties of biomacromolecules, their composition, and principles of their three-dimensional architecture. While all the above-mentioned methods will be covered, the in-depth emphasis will be on the determination of protein structure and dynamics in solution using NMR. The students will learn NMR pulse sequence design (including product operator formalism), principles of multidimensional NMR, methods for protein signal assignment and structure calculation, studies of protein-ligand interactions, and NMR approaches to protein dynamics. In addition to theoretical studies the students will get hands-on experience in NMR data analysis and in simulation of the outcome of NMR experiments on a computer.

Prerequisites: calculus, undergrad. biochemistry and physical chemistry.


Web Site for Protein Data Base:
Web site for Virtual NMR Spectrometer:
Lecture 21
Lecture 22
Lecture 23
Lecture 24

To Fushman Lab homepage