BCMB 401 — Protein Chemistry I
Biochemistry, Cell and Molecular Biology · University of Ghana
Primary structure: amino acid composition of proteins, determination of amino acid sequence, importance of primary structure synthesis of peptides, covalent modification of polypeptides. Secondary structure (regular arrangement of the polypeptide backbone): peptide bond and its structural implications; random polymers; Ramachandran Plot. Regular conformation of - -pleated sheets, other helices (310- helix), super-secondary structures (coiled- - -keratins, silk fibroin, collagen. Tertiary structure (folded conformation of globular proteins): determination of protein structure by X-ray crystallography, evidence for folding, reverse turns ( -turns) super-secondary structures (motifs), domains, interiors and exteriors, unfolding and folding. Example: Myoglobin. Quaternary structure (aggregation of globular proteins). Example: haemoglobin. Physical forces responsible for maintaining structure.
- Credits
- 2
- Level
- Level 400
- Semester
- Semester One
Other courses on this programme
- BCMB 400 — Project
- BCMB 402 — Protein Chemistry II
- 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).