lecture_10 - Protein Secondary Structure Lecture 2/19/2003...

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Protein Secondary Structure Lecture 2/19/2003
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Three Dimensional Protein Structures Confirmation: Spatial arrangement of atoms that depend on bonds and bond rotations. Proteins can change conformation, however, most proteins have a stable “native” conformation. The native protein is folded through weak interactions: a) hydrophobic interaction b) Hydrogen bonds c) Ionic bonds d) Van der Waals attractions
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A Denatured protein is unfolded, random dangling, and often precipitated (cooking egg whites). The Native conformation is dictated by its amino acid sequence. primary structure is everything. A one dimensional strand of DNA contains four dimensional data: height width depth life span!!
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The Amide bond Linus Pauling and Corey determined the structure of the peptide bond by X-ray. C O N C O N H - + 40% double bond character. The amide bond or peptide bond C-N bond is 0.13A ° shorter than C α -N bond. The carbonyl bond is .02 A ° longer then those for ketones and aldehydes
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This note was uploaded on 02/22/2011 for the course BCHS 3304 taught by Professor Johnson during the Spring '08 term at University of Houston.

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lecture_10 - Protein Secondary Structure Lecture 2/19/2003...

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