Sequence control of Aggregation Some Examples. Domain Swapping.

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Presentation transcript:

Sequence control of Aggregation Some Examples

Domain Swapping

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Loop-Sheet Insertion

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The ubiquitous crystallins  - large polydisperse complexes, molecular chaperone activity  - oligomeric, two domain structure,  B2 dimerizes by domain swapping  - monomeric, similar domain structure as  -crystallins Slingsby and Jaenicke (1999) Eye, Pt 3b:

Human  D-crystallin Fluorescence emission spectra Trp68 Trp42 Trp156 Trp130

Equilibrium Unfolding/Refolding in GdnHCl at 37 o C Refolding Unfolding

Folding pathway of H  D-Crys

Refolding: AFM Time Course 5 minutes 30 seconds 24 minutes54 minutes Native 300 nm 1  m

Hydrophobic domain interface residues N-terminal domainC-terminal domain Phe56 - Phe 80%, Val 8.5%, Ile 8.5%, Leu 3% Val131 - Val 54.3%, Ile 28.5%, Leu 17.2% Ile81 - Ile 80%, Val 8.5%, Leu 5.5%, Pro 3%, Thr 3% Leu144 - Leu 68.5%, Tyr 20%, Phe 11.5% Met43 - Met 77%, Val 11.5%, Ala 8.5%, Ile 3% Val169 - Val 49%, Ile 42%, Ala 3%, Met 3%, Leu 3% Conservation among 35  -crystallin sequences: N-terminal Met43 Phe56 Ile81 C-terminal Leu144 Val131 Val169

Equilibrium unfolding/refolding F56AV131A

Unfold at 2.3 M GuHCl Dilute to M GuHCl Measure Solution Turbidity at 350 nm Native control Refolded to 0.23 M GuHCl 10  g/ml protein 100  g/ml protein Refolding from intermediate

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