1 / 38

Chapter 3 Proteins

Chapter 3 Proteins. Purpose. Mostly for structure: skin, muscle, fingernails, hair. What is the “R” group?. Variable part of the amino acid Amino Acid Chart (handout). Forming/Breaking Peptide Bonds. 0. Type of Proteins. 8. Receptor Proteins Intercellular communication

keith-hall
Download Presentation

Chapter 3 Proteins

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript

  1. Chapter 3Proteins

  2. Purpose • Mostly for structure: skin, muscle, fingernails, hair

  3. What is the “R” group? • Variable part of the amino acid • Amino Acid Chart (handout)

  4. Forming/Breaking Peptide Bonds

  5. 0

  6. Type of Proteins • 8. Receptor Proteins • Intercellular communication • Bind to specific proteins (like hormones) • Receptor Proteins

  7. Note the H-bonds (between -O of carbonyl and -H of amino):coiling and pleating

  8. Tertiary Folding: disulfide bridges • Disulfide bridges formed between cysteine amino acids • (Look at cysteine’s structure)

  9. Disulfide Bridges • Formed when cysteine’s sulfur join • You Tube Videos Disulfide Bonds

  10. Use the Amino Acid Reference Sheet • Select the type of tertiary interaction as • (1) disulfide (2) ionic • (3) H bonds (4) hydrophobic • A. Leucine and valine • B. Two cysteines • C. Aspartic acid and lysine • D. Serine and threonine

  11. ANSWERS • 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

  12. Fibrous Strands Like hair, nails,skin, muscle fibers Globular Blobs Like hemoglobin, insulin, hormones, antibodies Two Basic Shapes

  13. Quaternary: combination of other shapes collagen

  14. 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

  15. Identify the level of protein structure • 1. Primary 2. Secondary • 3. Tertiary 4. Quaternary • ANSWERS • 2 Beta pleated sheet • 1 Order of amino acids in a protein • 4 A protein with two or more peptide • chains • 3 The shape of a globular protein • 3 Disulfide bonds between R groups

  16. Video Stuff • Protein Denaturation Video (McGraw-Hill) • Interactive Animations: Protein Folding • Protein Structures Animation • No Sound,but great molecular models

  17. Denaturation • Disruption of 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. NOTE: • Denaturation does not break the primary structure • Denaturation of an egg with a strong acid video

  19. Protein Extra Credit OPP • Can bring in up to 5 labels (no repeats) for 1 point each with a protein term circled: • protein • peptide • amino

  20. Proteins are Active • DO PROTEIN ACTIVITY

More Related