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Key to instructor resource annotations (shown to the right of or below outline topics):
PL = Available on Power Lecture DVD-ROM (ISBN 0538797592): V = video
TRA = Transparency acetates: 12e TRA = 12th edition, 11e TRA = 11th edition, 10e TRA = 10th edition
Introductory/whole chapter resources: PL figure JPEGs; Test Bank; IM WS 6-4, CA 6-1
I. The Chemist’s View of Proteins
Proteins are made from 20 different amino acids, 9 of which are essential. Each amino acid has an amino
group, an acid group, a hydrogen atom, and a side group. It is the side group that makes each amino acid
unique. The sequence of amino acids in each protein determines its unique shape and function.
A. Amino Acids 10e TRA 58, 59; IM WS 6-2
1. Amino acids have unique side groups that result in differences in the size, shape, and electrical charge
of an amino acid.
2. Nonessential amino acids, also called dispensable amino acids, are ones the body can create.
Nonessential amino acids include alanine, arginine, asparagines, aspartic acid, cysteine, glutamic acid,
B. Proteins 10e TRA 60
1. Amino acid chains are linked by peptide bonds in condensation reactions.
2. The sequence of amino acids that determines the structure of a protein varies greatly. Unlike
3. Weak electrical attractions within a polypeptide chain determine the secondary structure of proteins.
4. Polypeptide Tangles – Tertiary Structure
5. Multiple Polypeptide Interactions – Quaternary Structures
6. Protein denaturation is the uncoiling of protein that changes its ability to function.
a. Proteins can be denatured by heat and acid.
b. After a certain point, denaturation cannot be reversed.
II. Digestion and Absorption of Protein
Stomach acid and enzymes facilitate the digestion of protein. It is first denatured, then broken down to
polypeptides. The small intestine continues to break down protein into smaller peptides and amino acids so it
can be absorbed.
A. Protein Digestion
1. In the Stomach