Syllabus
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Course Code: BCH-103 Course Name: Proteins and Proteomics |
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| MODULE NO / UNIT | COURSE SYLLABUS CONTENTS OF MODULE | NOTES |
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| 1 | Primary structure of proteins: An overview of protein structure; hierarchy of protein structure; Ramachandran plot; Determination of primary structure of protein – determination of N and C-terminal residue; Determination of amino acid composition of protein and determination of sulfhydryl groups; location of disulfide bonds; Chemical synthesis of peptides; Structure and function of some biologically important polypeptides. Secondary and tertiary structure of proteins:Alpha helix and beta structure; Collagen helix and other types of helical structures; Super secondary structures; Amino acid sequence and three dimensional structure; Domains; Forces stabilizing the secondary and tertiary structure | |
| 2 | Sequencing, protein folding and denaturation: Protein sequencing; Sequenators;Quaternary structure of protein; Structure and function of hemoglobin and cytochrome c; Denaturation and renaturation of proteins; Characteristics of molten globule state; Proteins involved in folding; Models of protein folding; Chaperones and Lavinthal paradox; Protein conformation and diseases. | |
| 3 | Protein purification and separation techniques: Protein purification; criteria of purity, and fold purification; Ion-exchange, gel-filtration and affinity chromatography techniques; High performance liquid chromatography (HPLC); Iso-electric focusing (IEF); Native-PAGE and SDS-PAGE; Detection and quantification of proteins in gels; Recovery of proteins from gels. |
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| 4 | Proteomics: Overview and tools; Two-dimensional PAGE; Protein spot detection; Mass spectrometry: matrix assisted laser desorption ionization MS, Electrospray ionization MS, and tandem MS for protein identification; Identification of protein-protein interactions; Protein complexes; X-ray crystallography; Transmembrane domains; Functional proteomics; Application of proteome analysis. | |
