E chapter 4 - Chapter 4 Lecture Outlines Protein Structure...

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Chapter 4 Lecture Outlines Protein Structure and Function Copyright © Garland Science 2010
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CHAPTER CONTENTS THE SHAPE AND STRUCTURE OF PROTEINS HOW PROTEINS WORK HOW PROTEINS ARE CONTROLLED HOW PROTEINS ARE STUDIED ESSENTIAL CONCEPTS
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THE SHAPE AND STRUCTURE OF PROTEINS • The Shape of a Protein Is Specified by Its Amino Acid Sequence • Proteins Fold into a Conformation of Lowest Energy • Proteins Come in a Wide Variety of Complicated Shapes • The Alpha Helix and the Beta Sheet Are Common Folding Patterns • Helices Form Readily in Biological Structures • Beta Sheets Form Rigid Structures at the Core of Many Proteins • Proteins Have Several Levels of Organization • Few of the Many Possible Polypeptide Chains Will Be Useful • Proteins Can Be Classified into Families • Large Protein Molecules Often Contain More Than One Polypeptide Chain • Proteins Can Assemble into Filaments, Sheets, or Spheres • Some Types of Proteins Have Elongated Fibrous Shapes • Extracellular Proteins Are Often Stabilized by Covalent Cross-Linkages
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Proteins carry multiple functions in a cell • Catalysis • Structural components •Transpor t • Motors and motility •S torage • Signals and signal integrators • Receptors and ligands
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Figure 4-9 Essential Cell Biology (© Garland Science 2010) Proteins can adopt a huge # of shapes, they are structurally complex and functionally sophisticated. How is this accomplished? Each protein has a unique amino acid sequence that determines its three dimensional shape and biological activity
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Figure 4-1 Essential Cell Biology (© Garland Science 2010) Amino acids are linked together by peptide bonds
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Figure 4-2 Essential Cell Biology (© Garland Science 2010) A protein is made of amino acids linked together into a polypeptide chain
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Figure 4-3 Essential Cell Biology (© Garland Science 2010)
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Figure 4-4 Essential Cell Biology (© Garland Science 2010) Long polypeptide chains are very flexible. An enormous # of folds could form because free rotation. Folding is constrained by different sets of weak no- covalent bonds.
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Figure 4-5 Essential Cell Biology (© Garland Science 2010) Stability of each folded shape is affected by the combined strength of a large # of non-covalent bonds, hydrophobic interactions, distribution of polar and non-polar amino acids
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Figure 4-6 Essential Cell Biology (© Garland Science 2010) Each protein normally folds into a single stable conformation (minimal free energy), hydrogen bonds help stabilize its folded shape
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Figure 4-7 Essential Cell Biology (© Garland Science 2010) The conformation of a protein is determined solely by its amino acid sequence Why does UREA at high [] unfold proteins?
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• A protein can fold into its correct conformation without outside help. However in a living cell folding a is
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E chapter 4 - Chapter 4 Lecture Outlines Protein Structure...

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