Aims & Learning Objectives:
Aims: To provide understanding of protein conformation in terms of noncovalent interactions between amino acid side chains, the thermodynamic principles underlying the protein folding problem. Also to provide understanding of the various physical methods available for the characterisation of biological macromolecules and their application to the study of protein conformation.
After taking this course the student should be able to:
* give a qualitative description of the interactions that maintain the native conformation of a protein and determine the stability of the native conformation
* appreciate the structural information that various spectroscopic techniques can give
* understand the structural information that various scattering and diffraction techniques can give.
Content:
Polypeptide chain folding, the role of non-covalent interactions, the protein folding process, denaturation and renaturation, protein conformational change, spectroscopic techniques (UV/visible/IR, Raman, circular dichroism, nmr, esr), scattering techniques (X-ray diffraction, solution scattering), Microscopy (optical and electron)
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