BCMB 402 — Protein Chemistry II
Biochemistry, Cell and Molecular Biology · University of Ghana
Protein-ligand Interactions: Binding sites of haemoglobin and myoglobin, binding of oxygen and carbon monoxide, micro-environment of the haem iron, the Hill Plot. Protein engineering. Allostery: interaction between binding sites. Theoretical models; the Mond-Wyman-Changeux (MWC) concerted mechanism, the Koshland-Nemethy-Filmer (KNF) sequential model. Allosteric properties of haemoglobin; molecular mechanism of cooperative binding of oxygen to haemoglobin, the Bohr effect, binding of 2, 3-bisphosphoglycerate (BPG). Mechanism of Enzyme Catalysis: General acid-base catalysis and covalent catalysis. Catalysis by coenzymes; pyridoxal phosphate, thiamine pyrophosphate, ATP, coenzyme A, NAD(P)+ , FAD/FMN. Structure and mechanism of action of selected enzymes. Examples; dehydrogenases, proteases, ribonuclease, lysozyme, glycolytic enzymes such as phosphofructokinase (PFK).
- Credits
- 2
- Level
- Level 400
- Semester
- Semester Two
Other courses on this programme
- BCMB 400 — Project
- BCMB 401 — Protein Chemistry I
- BCMB 403 — Molecular Biotechnology & Applications
- BCMB 404 — Immunology and Immunochemistry
- BCMB 405 — Cell Signalling
- BCMB 406 — Molecular Genetics
- BCMB 407 — Cell & Molecular Biology Practical Ii
- BCMB 408 — Entrepreneurship For Innovations In Biosciences
- BCMB 409 — Biochemistry of Parasites
- BCMB 410 — Seminars and Scientific Writing
- BCMB 411 — Clinical Biochemistry
- BCMB 414 — Plant Biochemistry
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Start freeCourse details from University of Ghana Volume 3 Handbook for the Bachelor's Degree: Course Descriptions for Programmes in the Sciences (2017).