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Protein structure
This document discusses the primary, secondary, tertiary, and quaternary structures of proteins. It defines each structure and provides examples. Primary structure refers to the sequence of amino acids in the polypeptide chain. Secondary structures include the alpha helix, beta pleated sheet, and triple helix. Tertiary structure describes the overall 3D shape of a protein formed by interactions between amino acid R groups. Quaternary structure involves proteins with two or more polypeptide chains. The document also covers protein hydrolysis, which breaks peptide bonds, and denaturation, which disrupts higher-order protein structures.
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Protein structure
- 1. Amino Acids, Proteins,and 1 Enzymes Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation
- 2. Primary Structure ofProteins The particular sequence of amino acids that is the backbone of a peptide chain or protein CH3 S CH2 2 CH3 H3N CH O C N H O CH3 CH C N H O SH CH C N H O CH C O-CH CH CH3 CH2 CH2 + Ala-Leu-Cys-Met
- 3. Secondary Structure –Alpha 3 Helix • Three-dimensional arrangement of amino acids with the polypeptide chain in a corkscrew shape • Held by H bonds between the H of –N-H group and the –O of C=O of the fourth amino acid along the chain • Looks like a coiled “telephone cord”
- 4. Secondary Structure –Beta 4 Pleated Sheet • Polypeptide chains are arranged side by side • Hydrogen bonds form between chains • R groups of extend above and below the sheet • Typical of fibrous proteins such as silk
- 5. Secondary Structure –Triple 5 Helix • Three polypeptide chains woven together • Glycine, proline, hydroxy proline and hydroxylysine • H bonding between –OH groups gives a strong structure • Typical of collagen, connective tissue, skin, tendons, and cartilage
- 6. Learning Check P1 Indicate the type of structure as (1) primary (2) alpha helix (3) beta pleated sheet (4) triple helix A. Polypeptide chain held side by side by H bonds B. Sequence of amino acids in a polypeptide chain C. Corkscrew shape with H bonds between amino 6 acids D. Three peptide chains woven like a rope
- 7. 7 Solution P1 Indicate the type of structure as (1) primary (2) alpha helix (3) beta pleated sheet (4) triple helix A. 3 Polypeptide chain held side by side by H bonds B. 1 Sequence of amino acids in a polypeptide chain C. 2 Corkscrew shape with H bonds between amino acids D. 4 Three peptide chains woven like a rope
- 8. Tertiary Structure •Specific overall shape of a protein • Cross links between R groups of amino acids in chain disulfide –S–S– + ionic –COO– H3N– H bonds C=O HO– hydrophobic –CH3 H3C– 8
- 9. Learning Check P2 Select the type of tertiary interaction as (1) disulfide (2) ionic (3) H bonds (4) hydrophobic 9 A. Leucine and valine B. Two cysteines C. Aspartic acid and lysine D. Serine and threonine
- 10. 10 Solution P2 Select the type of tertiary interaction as (1) disulfide (2) ionic (3) H bonds (4) hydrophobic A. 4 Leucine and valine B. 1 Two cysteines C. 2 Aspartic acid and lysine D. 3 Serine and threonine
- 11. Globular and FibrousProteins Globular proteins Fibrous proteins “spherical” shape long, thin fibers Insulin Hair Hemoglobin Wool Enzymes Skin Antibodies Nails 11
- 12. Quaternary Structure •Proteins with two or more chains • Example is hemoglobin Carries oxygen in blood Four polypeptide chains Each chain has a heme group to 12 bind oxygen
- 13. Learning Check P3 Identify the level of protein structure 1. Primary 2. Secondary 3. Tertiary 4. Quaternary A. Beta pleated sheet B. Order of amino acids in a protein C. A protein with two or more peptide chains D. The shape of a globular protein E. Disulfide bonds between R groups 13
- 14. 14 Solution P3 Identify the level of protein structure 1. Primary 2. Secondary 3. Tertiary 4. Quaternary A. 2 Beta pleated sheet B. 1 Order of amino acids in a protein C. 4 A protein with two or more peptide chains D. 3 The shape of a globular protein E. 3 Disulfide bonds between R groups
- 15. Protein Hydrolysis 15 • Break down of peptide bonds • Requires acid or base, water and heat • Gives smaller peptides and amino acids • Similar to digestion of proteins using enzymes • Occurs in cells to provide amino acids to synthesize other proteins and tissues
- 16. Hydrolysis of aDipeptide OH CH2 O 16 CH3 H3N CH O C N H OH CH2 O CH C OH + CH3 heat + + H3N CH O COH H2O, H+ + CH C H3N OH
- 17. 17 Denaturation Disruptionof secondary, tertiary and quaternary protein structure by heat/organics Break apart H bonds and disrupt hydrophobic attractions acids/ bases Break H bonds between polar R groups and ionic bonds heavy metal ions React with S-S bonds to form solids agitation Stretches chains until bonds break
- 18. Applications of Denaturation • Hard boiling an egg • Wiping the skin with alcohol swab for injection • Cooking food to destroy E. coli. • Heat used to cauterize blood vessels • Autoclave sterilizes instruments • Milk is heated to make yogurt 18
- 19. Learning Check P4 What are the products of the complete hydrolysis of Ala-Ser-Val? 19
- 20. 20 Solution P4 The products of the complete hydrolysis of Ala-Ser-Val are alanine serine valine
- 21. Learning Check P5 Tannic acid is used to form a scab on a burn. An egg becomes hard boiled when placed in hot water. What is similar about these two events? 21
- 22. 22 Solution P5 Acid and heat cause a denaturation of protein. They both break bonds in the secondary and tertiary structure of protein.