drake6 - Higher Order Protein Structures Lecture 6, Medical...

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Higher Order Protein Structures Lecture 6, Medical Biochemistry
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Lecture 6 Outline Molecular forces involved in protein structure Protein folding Structure and biosynthesis of collagen
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Protein Native State and Denaturation A protein folded into its tertiary structure under optimal conditions is said to be in its “native state,” which corresponds to its most thermo- dynamically favorable arrangement of atoms. Proteins can be denatured (loss of their secondary and higher structures) by changes in temperature, pH, ionic strength, urea or detergents
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Proposed Folding Pathway Accessory proteins?
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O-H = 460 C-H = 410 C-C = 350 Bond kJ/m Compare:
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Non-covalent Molecular Forces in Protein Structure and Folding Hydrophobic interactions : interactions between hydrophobic amino acids is likely the largest noncovalent force responsible for most protein folding. Recall that water will tend to form a solvation shell around free hydrophobic compounds, which in thermodynamic terms, is a decrease in entropy (and thus not favored). This drives formation of hydrophobic regions of protein chains to come together, the water shell is disrupted and entropy increases.
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Non-covalent Forces (cont) For hydrophobic interactions, calculations have shown that 1/3 loss of water of solvations occurs with formation of secondary structure; an additional 1/3 water of solvation is lost in the formation of tertiary structure. This is a large source of the energy
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This note was uploaded on 12/16/2011 for the course BIOLOGY 101 taught by Professor Mr.wallace during the Fall '11 term at Montgomery College.

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drake6 - Higher Order Protein Structures Lecture 6, Medical...

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