FDST 100 Lecture Notes - Lecture 5: Isoleucine, Beta Sheet, Tryptophan
27 Jan 2017
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Document Summary
Large biomolecules consisting of one or more chains of amino acid residues that are significant in complexity and functionality. In every living cell in the body. Important nutrient, particularly in regards to muscle, skin and bone development and maintenance. Contains at least 16% nitrogen: c,h,o and n, sometimes s (sulphur) Create the structure of hormones, enzymes and antibodies. Peptides (20-30 amino acids: also known as oligopeptides. Produce some, consume others: 9 essential (must consume, 11 nonessential (body synthesizes) Primary: just aa in linear chain with covalent bonds. Secondary: beta sheets and alpha helix, folding and coiling caused by hydrogen bonding. Tertiary: 3d structure, covalent, ionic and hydrogen bonding. Solubility: based off amino acid content. Lactalbumin and ovalbumin vs keratin and collagen. Water binding: some proteins bind water forcing h-bonds. Denaturing: fragile no matter the structure, loss in biological activity, changes in physical/functional properties, like solubility. Complete amino acids: meat, poultry, fish. Non complete: dairy, certain grains, beans.
