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lecture 9 - 9-1 Forces Governing Protein Structure...

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Forces Governing Protein 9-1
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9-2 MCB354 Lecture 9 Reading in Lehninger : Chapter 2 , pp. 47-51; Chapter 4 , pp. 113-115; 140-143 MVLSEGEWQLVLHVWAKVEAD VAGHGGDILIRLFKSHPETL EKFDRFKHLKTEAEMKASED LKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIP IKYLEFISEAIIHVLHSRHP GDFGADAQGAMNKALELFRK DIAAKYKELGYGG WHY FAVORED? WHAT FORCES ARE INVOLVED? Forces Governing Protein Structure Protein Denaturation
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Review of Weak Forces Covalent bonds Ionic interactions Ion-dipole interactions Van der Waals interactions Hydrogen bonds Hydrophobic interactions 9-3
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Review of Weak Forces Covalent bonds Ionic interactions Ion-dipole interactions Van der Waals interactions Hydrogen bonds Hydrophobic interactions 9-3
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9-4
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intermediates Native Structure Totally Denatured (many states) Energy 9-5
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9-6
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9-7
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9-8
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9-9 Enthalpy component in protein folding/denaturation Energy of non-covalent interactions within the polypeptide chain H-BONDS IONIC INTERACTIONS Van der Waals H reflects breakage or formation of these interactions Must also consider covalent disulfide bonds S-S; this is usually the only covalent bond change to consider in protein denaturation
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9-10
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9-11
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Temperature Changes the Natured/Denatured Equilibrium 9-12 G ( kcal/mol ) Temperature
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1. H-bonds (“polar” interactions) 2. Hydrophobic interactions (“non-polar” ) 3. Van der Waals forces (dipole-dipole interactions) 4. Ionic interactions (salt bridges) - The weak or non-covalent interactions that stabilize the native conformation of proteins are…. . - The result of the cumulative effect of many “weak” or “non-covalent” interactions (also, S-S bridges) between main chain polar groups and side chain groups within the polypeptide - These interactions, which take place in aqueous solution, counteract interactions between groups on the polypeptide and water molecules Stabilization of a protein’s conformation 9-13
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lecture 9 - 9-1 Forces Governing Protein Structure...

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