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SURVEY OF BIOCHEMISTRY Protein Function PowerPoint Presentation
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SURVEY OF BIOCHEMISTRY Protein Function

SURVEY OF BIOCHEMISTRY Protein Function

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SURVEY OF BIOCHEMISTRY Protein Function

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  1. SURVEY OF BIOCHEMISTRYProtein Function

  2. PRS In a protein, the most conformationally restricted amino acid is_____ and the least conformationally restricted amino acid is ________. • Trp, Gly • Met, Cys • Pro, Gly • Ile, Ala

  3. PRS In a protein, the most conformationally restricted amino acid is_____ and the least conformationally restricted amino acid is ________. • Trp, Gly • Met, Cys • Pro, Gly • Ile, Ala

  4. PRS The arrangement of the regular structural elements and the positions of atoms in the protein are considered part of the ______. • Primary structure • Secondary structure • Tertiary structure • Quaternary structure

  5. PRS The arrangement of the regular structural elements and the positions of atoms in the protein are considered part of the ______. • Primary structure • Secondary structure • Tertiary structure • Quaternary structure

  6. PRS Lysine can form a salt bridge by associating with a nearby ____ residue. • Pro • Ser • Gln • Glu

  7. PRS Lysine can form a salt bridge by associating with a nearby ____ residue. • Pro • Ser • Gln • Glu

  8. PRS Noncovalent forces that stabilize protein structure include all of the following except _______. • The hydrophobic effect • Salt bridges • Disulfide bridges • Metal-ion coordination

  9. PRS Noncovalent forces that stabilize protein structure include all of the following except _______. • The hydrophobic effect • Salt bridges • Disulfide bridges • Metal-ion coordination

  10. PRS Which of the following DNA sequences is (are) palindromic? • AGCT • AAGNCTT • AGGA • #1 and #2

  11. PRS Which of the following DNA sequences is (are) palindromic? • AGCT • AAGNCTT • AGGA • #1 and #2 5’-AGCT-3’ 3’-TCGA-5’ 5’-AAGNCTT-3’ 3’-TTCNGAA-5’ 5’-AGGA-3’ 3’-TCCT-5’

  12. Protein Function: Overview Chapter 7 - with emphasis onMyoglobin and Hemoglobin • Transport • Contraction • Protection • Catalysis • Regulation • Gene regulation • Hormonal regulation • Structural Support

  13. Why focus on Mb and Hb? BiologicalImportance

  14. Why focus on Mb and Hb?

  15. Why focus on Mb and Hb? • Biological Importance • Role in Transport of O2 • Myoglobin: O2 transport to muscles • Hemoglobin: O2 transport from lungs • Ligand Binding • Simple binding • Cooperativity and Allosteric Interactions

  16. Ligand Binding: General Concepts • How can ligand binding be: • Described? • Measured? • Regulated? • Distinctions between binding categories • One Protein + One Ligand • One Protein + Multiple Ligands

  17. Heme is what O2 binds Heme is a porphyrin prosthetic molecule

  18. Myoglobin and Hemoglobin Mb- O2 Hb- O2 Myoglobin Hemoglobin 1 4 1 4 8 8 # subunits# heme groups# Alpha Helices 18% identical residues

  19. Structure Changes on Binding Fig 6-38 shows Mb “breathing” How is O2 binding to Mbdescribed? Show on board…

  20. O2 Binding to Myoglobin Shape indicatessimple binding ofO2 to Mb

  21. Hb has 2 conformations Without O2T State With O2R State

  22. O2 Binding to Hemoglobin Arteries carry oxygenated blood Veins carry deoxygenated blood

  23. Upcoming… • More on Hb and Mb on Friday • General concepts • Muscle Contraction • Antibodies • Exam #1 on Thursday • Boggs B6A 4-5 pm