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GPCR Edition – Week 1

GPCR Edition – Week 1. Amino Acid Structure. Amino Acids: Misc. GPCR Structure. Chemical Interactions. Protein Secondary & Tertiary Structure. Potpourri. 100. 100. 100. 100. 100. 100. 200. 200. 200. 200. 200. 200. 300. 300. 300. 300. 300. 300. 400. 400. 400. 400. 400.

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GPCR Edition – Week 1

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  1. GPCR Edition – Week 1

  2. Amino Acid Structure Amino Acids: Misc. GPCR Structure Chemical Interactions Protein Secondary & Tertiary Structure Potpourri 100 100 100 100 100 100 200 200 200 200 200 200 300 300 300 300 300 300 400 400 400 400 400 400 500 500 500 500 500 500

  3. Glycine

  4. Valine

  5. Cysteine

  6. Histidine

  7. Tryptophan

  8. The amino acid arginine has this grouping of amino acids, along with lycine and histidine (if the pH is just right) Positively charged

  9. This amino acid can be abbreviated as “Gln” or “Q” Glutamine

  10. The amino acid arginine is abbreviated as “Arg” as well as this one letter R

  11. “alpha” refers to this element that is covalently bonded to an amino group, a carboxyl group, a hydrogen, and a side chain Carbon

  12. This number is the net negative or positive charge of the following short oligopeptide: DEKHR +1

  13. GPCRs are also known as hetpahelical receptors, meaning they have this number of alpha helices seven

  14. GPCRs are embedded into a membrane bilayer composed of this type of biological molecule Phospholipid

  15. GPCRs are very difficult to crystallize and often times have crystallization “handles” fused to them. This one is similar to what we used in our experiment. T4 Lysozyme

  16. This class of GPCRs has a large extracellular domain with a “venus-flytrap” structure where ligands bind Class C

  17. Class A GPCRs have this conserved sequence motif of three amino acids that mediates coupling to G proteins DRY, Asp-Arg-Tyr

  18. The attraction of a cation to an anion is referred to as this type of non-covalent chemical interaction Ionic/Electrostatic

  19. The non-covalent interaction shown here Hydrogen Bond

  20. This non-covalent is what drives non-polar amino acids to orient themselves towards the interior of a protein and away from water Hydrophobic Effect

  21. A peptide bond is a covalent chemical interaction between the amino group of one amino acid and this group of the other Carboxyl

  22. DAILY DOUBLE Hydrogen bonding between the carbonyl oxygen and amino group hydrogen of two amino acids 4 residues apart stabilizes this type of structure Alpha helix

  23. This is the simplest arrangement a polypeptide chain can make in terms of secondary structure Alpha Helix

  24. This amino acid’s rigidity results in its low probability of being found in an alpha helix Proline

  25. The partial positive and negative charge of an alpha helix N- and C-terminus, respectively, is referred to as this Helix Dipole

  26. This is the name of the chart that measures the probability of particular psi and phi angles to be found in secondary structure Ramachandran

  27. This protein structural motif is named after a common architectural design found in the Hellenic Republic Greek Key Motif

  28. This level of protein structure is the arrangement of 2 or more separate polypeptide chains (subunits) Quaternary

  29. GPCRs are composed primarily of this type of secondary structure Alpha Helix

  30. The functional and folded structure of a protein in its normal environment is known as this Native conformation

  31. The formation of a peptide bond between two amino acids results in the creation of this molecule, which is why the reaction is called condensation Water

  32. Which university is the only one in NCAA history to hold the national title in both basketball and football? University of Florida

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