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SURVEY OF BIOCHEMISTRY Protein Function

This survey of biochemistry focuses on protein function, including the conformational restrictions of amino acids, protein structure, salt bridges, noncovalent forces, and DNA palindromes. It also explores the importance of myoglobin and hemoglobin in biological systems, ligand binding, and the role of heme in oxygen transport.

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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

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