Chemistry 402 » Spring (even years) » Full Semester
4 Credits
Bio-Physical Chemistry I
Instructor(s): Douglas H. Turner

Prerequisites: 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

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