DTN102 Lecture Notes - Lecture 3: Ionic Bonding, Globular Protein, Hydrogen Bond

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5 Mar 2019
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Functions in the body and food sources of proteins: protein has many functions in the body including growth and maintenance, enzymes, hormones, regulation of fluid balance, acid base regulation, transport molecules, antibodies, and as an energy source. Food sources of proteins include animal proteins such as meat, milk, fish, and eggs and plant source such as legumes, and nuts. Proteins perform a range of functions in foods: hydration, browning, denaturation/coagulation, enzymatic reactions, thickening, buffering. Examples are collagen in connective tissue and tendons, and keratin in wool, hair, and nails: globular proteins, which are soluble. An example is insulin, a hormone involved in glucose metabolism and controlling blood glucose levels: myoglobin and haemoglobin, involved in oxygen transport. Types of bonding: hydrogen bonds, covalent bonds, disulphide bonds/links (important in protein structure, dispersion forces/hydrophobic interactions, dipole-dipole forces, van der waals forces. Includes a simple view of ionic bonding and the way you need to modify this for a"level purposes.

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