Department of Biology & Biochemistry, Unit Catalogue 2009/10 |
BB20020: Physical biochemistry & proteins |
 Credits:
| 6 |
| Level:
| Intermediate |
| Period: | Semester 1 |
| Assessment:
| EX 80%, PR 20% |
| Supplementary Assessment: | Like-for-like reassessment (where allowed by programme regulations) |
| Requisites:
| Before taking this unit you must take BB10003 and take BB10004 and take CH10088 and take CH10087 |
| Description: | Aims: This unit will explore the concept of protein conformation in terms of non-covalent interactions between amino acid side chains and consider the thermodynamic principles underlying the protein folding problem. It will also introduce various physical methods available for the characterisation of biological macromolecules and their application to the study of protein conformation. Learning Outcomes: After taking this course the student should be able to: * Describe qualitatively the interactions that determine the native conformation of a protein and its stability. * Describe the process and application of spectroscopic and diffraction techniques to the investigation of molecular structures and assemblies. * Compare the relative advantages and limitations of different structural techniques and propose appropriate experiments for given structural questions. * To manipulate, and calculate values from, the Beer-Lambert law and basic thermodynamic formulae. Skills: Learning and studying T/F/A, Written communication T/F/A, Numeracy & computation T/F/A, Laboratory skills T/F, Information technology T/F, Information handling & retrieval T/F/A, Working independently T/F. Content: Protein structure: polypeptide chain folding, the role of non-covalent interactions, the protein folding process, denaturation and renaturation, protein conformational change. Main techniques taught: spectroscopic techniques (UV, fluorescent, circular dichroism, NMR, ), X-ray diffraction and electron microscopy. |