《Biophysical Chemistry》course for undergraduates/graduates

Credit: 2;  Class hours: 32. 

Lecturers: Prof. Luhua Lai & Prof. Zhirong Liu.

Aims:

    To develop an intuitive, practical understanding of the principles necessary for a physical understanding of biochemical processes, and to develop an appreciation of the utility of quantitative information.

References:

1. Biophysical Chemistry, Alan Cooper, The Royal Society of Chemistry, 2004

2. Principles of Physical Biochemistry, K.E. van Holde, W.C. Hohnson, R.S. Ho, Prentice-Hall, Inc., 1998

3. Molecular Biophysics, M. Daune, Oxford University Press, 1999

4. Luhua Lai, Protein structure prediction and molecular design. (Peking University Press, Beijing, 1993).

Contents:

1. Biological macromolecules: composition, structure and conformation

— Biophysical and chemical properties of the 20 amino acids;

— The chemical composition, hierarchical structure and folding type of protein;

— DNA: double helix, tertiary structure, A-, B-, Z-type, tetrad structure, linear and circular, super helix;

— RNA: type, nature and comparison with DNA;

— Structure determination: XRD and NMR;

— Prediction of protein secondary and tertiary structure;

2. Dynamic behaviors of biomolecules and their properties in solution

— Atomic fluctuations and nomal mode analysis;

— Diffusion, Brownian motion and the influence of external field;

— Dltracentrifugation technology;

— Dynamic light scattering;

3. Conformational transition and molecular binding

— Statistical properties of Coils

— Secondary structure and helix-coil transition;

— The single-double-strand transition, B-Z transition and worm-like model of DNA;

— Denaturation and folding of protein;

— Hydration: hydrophobic and hydrophilic;

— Molecular binding: bimolecular system, multiple binding sites, enzymatic reaction and Michaelis equation;

4. Physichemical methods in biological testing

— UV and fluorescence spectroscopy;

—Circular dichroism;

— Thermodynamic properties: calorimetry;

— Kinetics: mixing technology, relaxation method, H-D exchange, surface plasmon resonance (SPR);

— Single molecule methods: atomic force microscopy, single molecule spectroscopy, electron microscopy;

5. Advanced topics

—Protein and drug molecular design.