Chemistry 402 » Spring (even years) » Full Semester
4 Credits
Bio-Physical Chemistry I
Instructor(s): Douglas H. TurnerPrerequisites: CHM 252 or equivalent.Crosslisting: None.Course Summary:
An introduction to the theory and practical application of several major techniques used in the structural characterization of biological macromolecules. These methods include: X-ray crystallography, Small Angle X-ray Scattering, Spectroscopic and Calorimetric Techniques, NMR and Comparative Modeling. The goal is to enable non-specialists to become conversant in the language and principles of the field, as well as to understand the strengths and limitations of various techniques. Prerequisites: Chem 252 or equivalent.
Course Topics:
- Overview of NMR as a spectroscopic method: Energies and time scales
- Spin magnetization, vector model, the rotating frame
- Chemical Shifts
- Relaxation: Description of T1 and T2 (vector model)
- NMR - applications
- Fluorescence Spectroscopy
- Calorimetry of Macromolecules
- Surface Plasmon Resonance
- Atomic Force Microscopy/Single Molecule FRET
- CD of Proteins/CD & UV of Nucleic Acids
- 2D NMR: NOESY, COSY, TOCSY
- 2D NMR: HETCOR, HMQC, HSQC
- Reciprocal Lattice & Laue Eqns.
- The Ewald Sphere
- The Phase Problem
- Solving the Phase Problem (I): from Patterson to Difference (DP) Maps
- Solving the Phase Problem (II): MIR
- What do I do with an Experimentally Phased Map? (Model Building)
- Short (and not so short) cuts: Difference Fourier, Molecular Replacement, Multi-Wavelength Methods for Phasing
- Crystallographic Symmetry and NCS & Map Fitting and Quality Indicators
- Protein & RNA Taxonomies
- Modern Structure Determination, Manipulation & Viewing of Coordinates
- Structural Genomics
- Small Angle Scattering with X-rays and Neutrons/Neutron Diffraction/EM