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A comprehensive overview of amino acids, peptides, and proteins, covering their structure, properties, classification, and functions. It delves into the central dogma of molecular biology and protein biochemistry, explaining the relationship between sequence, structure, and function. The document also explores the different levels of protein structure, including primary, secondary, tertiary, and quaternary structures, and the bonds that stabilize these structures. Additionally, it discusses the denaturation of proteins and the factors that can cause it. Finally, the document examines the classification of proteins based on shape, composition, and function, providing examples of each type.
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Amino acids, peptides
and proteins
Learning objectives of Part I
4
Glycine, the only amino acid with a hydrogen atom as a side chain
Proline contains a secondary amine group (– NH- ), called an imine, instead of a primary amine group (-NH 2 )
Optical properties of amino acids
Acid/base properties of amino acids
A titration curve for glycine. The pH controls the charge on glycine: cationic below pH 2.3; zwitterionic between pH 2.3 and 9.6; and anionic above pH 9.6. The isoelectric pH is 6.0.
indispensable amino acids
dispensable amino acids
Classification of amino acids based on nutritional requirement
Classification of amino acids based on metabolic fate