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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
http://personal.tmlp.com/Jimr57/textbook/chapter2/ps1a.htm • • 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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- Fall '09