|
 Academic Year:
| 2015/6 |
| Owning Department/School:
| Department of Biology & Biochemistry |
| Credits:
| 6 |
| Level:
| Intermediate (FHEQ level 5) |
| Period: |
Semester 1 |
| Assessment Summary:
| EX 80%, PR 20% |
| Assessment Detail: |
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| Supplementary Assessment: |
Like-for-like reassessment (where allowed by programme regulations) |
| Requisites: | Before taking this module you must take BB10003 AND take BB10121 AND take CH10088 AND take CH10087 |
| Description:
| Aims: To provide basic understanding of the factors that cause a protein to fold and the properties of those folds. To explore current methods for determining protein structures, folds and assemblies. 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 form, occurrence and function of protein folds * 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 these techniques and the data they provide. * Propose appropriate experiments for given structural questions. 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, Group working T/F. Content: Principles of protein folding Protein folds Methods and application of X-ray crystallography Methods and application of NMR spectroscopy Application of structural data to medicine and drug discovery. |
| Programme availability: |
BB20020 is Compulsory on the following programmes:Department of Biology & Biochemistry
BB20020 is Optional on the following programmes:Department of Biology & Biochemistry
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