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. 1998 Jul;7(7):1545–1554. doi: 10.1002/pro.5560070708

Engineering of betabellin-15D: a 64 residue beta sheet protein that forms long narrow multimeric fibrils.

A Lim 1, M J Saderholm 1, A M Makhov 1, M Kroll 1, Y Yan 1, L Perera 1, J D Griffith 1, B W Erickson 1
PMCID: PMC2144068  PMID: 9684887

Abstract

The betabellin target structure is a beta-sandwich protein consisting of two 32 residue beta-sheets packed against one another by interaction of their hydrophobic faces. The 32 residue chain of betabellin-15S (HSLTAKIpkLTFSIAphTYTCAV pkYTAKVSH, where p=DPro, k=DLys, and h=DHis) did not fold in water at pH 6.5. Air oxidation of betabellin-15S provided betabellin-15D, the 64 residue disulfide bridged two-chain molecule, which also remained unfolded in water at pH 6.5. By circular dichroic spectropolarimetry, the extent of beta structure observed for betabellin-15D increased with the pH and ionic strength of the solution and the betabellin-15D concentration. By electron microscopy, in 5.0 mM MOPS and 0.25 M NaCl at pH 6.9, betabellin-15D formed long narrow multimeric fibrils. A molecular model was constructed to show that the dimensions of these betabellin-15D fibrils are consistent with a single row of beta-sandwich molecules joined by multiple intersheet H-bonds.

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Selected References

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