Biophysical characterization of betabellin 16D: a beta-sandwich protein that forms narrow fibrils which associate into broad ribbons.
The betabellin structure is a de novo designed beta-sandwich protein consisting of two 32-residue beta sheets packed against one another by hydrophobic interactions. Betabellin 16S (B16S), a 32-residue peptide chain (HSLTAKIakLTFSIAahTYTCAVakYTAKVSH, where a is DAla, h is DHis, and k is DLys), did not have beta structure in water at pH 6.5. Air oxidation of B16S furnished betabellin 16D (B16D), a 64-residue disulfide-bridged two-chain protein, which also did not fold in water at pH 6.5. However, the extent of beta structure observed for B16D increased with pH and ionic strength of the solution and the B16D concentration as observed by circular dichroism spectropolarimetry. Transmission electron microscopy showed that B16D formed narrow fibrils that associated into broad ribbons in 5.0 mM Mops and 0.25 M NaCl at pH 6.9.
Lim
A
A
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA. amareth@bu.edu
Makhov
A M
AM
Saderholm
M J
MJ
Griffith
J D
JD
Erickson
B W
BW
D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D009994:Osmolar Concentration; D015202:Protein Engineering; D017510:Protein Folding; D017433:Protein Structure, Secondary
D009842:Oligopeptides; C400381:betabellin 16D