233Chapter8.1_Protein_Structure_2(2)

233Chapter8.1_Protei - Chemistry 233 Fundamentals of Biochemistry Protein Structure 2 Another structural protein Silk Fibroin Structure silk has

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Unformatted text preview: Chemistry 233 Fundamentals of Biochemistry Protein Structure 2 Another structural protein: Silk Fibroin Structure silk has regions of β-sheet structure with alternating Gly and Ala residues the alternating Gly and Ala side chains fit together and hold the β-sheets together Collagen Highly Repeating structure: Hyp and Hyl residues necessary for proper collagen structure proline and lysine residues are hydroxylated after protein synthesis, requiring ascorbic acid left-handed helix, 3.3 residues per turn, pitch = 2.86 nm . The triple helix of collagen. 3 left-handed helices form a right-handed helix → “tropocollagen” small Gly residues are small enough to fit inside the helix H-bonding with Gly amide N-H holds tropocollagen together 8-30b X-Ray structure of the triple helical collagen many tropocollagen helices make a collagen fiber electron micrograph of collagen fiber intra- and intermolecular crosslinking via Lys and His residues Globular Proteins globular proteins have tertiary (3...
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This note was uploaded on 03/12/2009 for the course CHEM 233 taught by Professor Daub during the Winter '09 term at Waterloo.

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233Chapter8.1_Protei - Chemistry 233 Fundamentals of Biochemistry Protein Structure 2 Another structural protein Silk Fibroin Structure silk has

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