Protein Chemistry Notes

O tertiary describes the overall three dimensional

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Unformatted text preview: hin a polypeptide. o Tertiary – describes the overall three dimensional shape achieved by the folding of the entire protein molecule. o Quaternary - more than one polypeptide chain in its spatial structure . Ex. Casein, collagen, myosin • • Denaturation – the unfolding of a protein structure, usually due to acid or heat o The normal spatial arrangements and the proteins functional properties are altered or lost when this occurs. o Examples: Cottage cheese is made by adding acid which causes coagulation to occur. Proteinprotein interaction takes place. Scrambled eggs change by heat. Food proteins are typically one of two shapes: o Globular – spherical like a ball Most are soluble in water Ex: Myoglobin o Fibrous – Elongated like a twisted rope Generally insoluble in water Globular Protein Structure Fibrous Protein Structure Ex: Collagen Functional Properties of Proteins Buffering – refers to preventing a pH change • The buffering ability of a protein is a function of the amino ac...
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