1. Chapter 5Proteins: Their Primary Structure and Biological Function
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2. ESSENTIAL QUESTIONSProteins are polymers composed of hundreds or even thousands of amino acids linked in series by peptide bonds.What structural forms do these polypeptide chains assume, how can the sequenceof amino acids in a protein be determined, and w
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3. 5.1 What Architectural Arrangements Characterize Protein Structure?Proteins Fall into Three Basic Classes According to Shape and Solubility
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4. 5.1 What Architectural Arrangements Characterize Protein Structure?
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5. 5.1 What Architectural Arrangements Characterize Protein Structure?
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6. 5.1 What Architectural Arrangements Characterize Protein Structure?
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7. 5.1 What Architectural Arrangements Characterize Protein Structure?
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8. Secondary Structure Through hydrogen-bonding interactions between adjacent amino acid residues, the polypeptide chain can arrange itself into characteristic helical or pleated segments. These segments constitute structural conformities, so-called regular
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9. Tertiary Structure When the polypeptide chains of protein molecules bend and fold in order to assume a more compact three-dimensional shape, the tertiary (3°) level of structure is generated (Figure 5.4). It is by virtue of their tertiary structurethat pr
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10. Quaternary Structure Many proteins consist of two or more interacting polypeptide chains of characteristic tertiary structure, each of which is commonly referred to as a subunit of the protein. Subunit organization constitutes another levelin the hierarch
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11. Noncovalent Forces Drive Formation of the Higher Orders of Protein Structure
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12. Figure 5.6 Configuration and conformation are not synonymous
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13. 5.2 How Are Proteins Isolated and Purified from Cells?
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14. 5.2 How Are Proteins Isolated and Purified from Cells?
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15. 5.2 How Are Proteins Isolated and Purified from Cells?
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16. Dialysis
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17. Chromatography
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18. Ion Exchange Chromatography Can Be Used to Separate Molecules on the Basis of Charge
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19. Ion Exchange Chromatography Can Be Used to Separate Molecules on the Basis of Charge
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20. Gel Filtration Chromatography Can Be Used to Separate Molecules on the Basis of Size
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21. Slide 21
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22. Affinity Chromatography
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23. Hydrophobic Interaction Chromatography
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24. High-Performance Liquid Chromatography
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25. Gel Electrophoresis
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26. SDS-Polyacrylamide Gel Electrophoresis (SDS-PAGE)
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27. Slide 27
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28. SDS-Polyacrylamide Gel Electrophoresis (SDS-PAGE)
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29. Two-Dimensional Gel Electrophoresis
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30. 5.3 How Is the Amino Acid Analysis of Proteins Performed?
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31. 5.4 How is the Primary Structure of a Protein Determined?
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32. In 1953, Sanger sequenced the two chains of insulin.Sanger's results established that all of the molecules of a given protein have the same sequence.Proteins can be sequenced in two ways:- real amino acid sequencing- sequencing the corresponding DNA in
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33. The sequence of insulin
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34. Determining the Sequence – A Six Step Strategy
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35. Determining the Sequence - A Six Step Strategy
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36. Step 1:
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37. Step 2:
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38. Disulfide cleavage
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39. Step 3:
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40. Reactions of Amino Acids
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41. Step 3:
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42. Reactions of Amino Acids
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43. Step 3:
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44. Enzymatic Fragmentation
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45. Enzymatic Fragmentation
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46. Slide 44
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47. Chemical Fragmentation
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48. Polypeptide Cleavage Procedures
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49. Step 6:
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50. Reconstructing a Sequence
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51. Reconstructing the Sequence of an Unknown Peptide