Genetic engineering combined with deep UV resonance Raman spectroscopy for structural characterization of amyloid-like fibrils.
Elucidating the structure of the cross-beta core in large amyloid fibrils is a challenging problem in modern structural biology. For the first time, a set of de novo polypeptides was genetically engineered to form amyloid-like fibrils with similar morphology and yet different strand length. Differential ultraviolet Raman spectroscopy allowed for separation of the spectroscopic signatures of the highly ordered beta-sheet strands and turns of the fibril core. The relationship between Raman frequencies and Ramachandran dihedral angles of the polypeptide backbone indicates the nature of the beta-sheet and turn structural elements.
Sikirzhytski
Vitali
V
Department of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, New York 12222, USA.
Topilina
Natalya I
NI
Higashiya
Seiichiro
S
Welch
John T
JT
Lednev
Igor K
IK
D000682:Amyloid / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D015202:Protein Engineering / Q000379:methods*; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman / Q000379:methods*
D000682:Amyloid; D010455:Peptides