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Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence.
The results indicate that Abeta in vivo is a metalloprotein, and the loosening of the structure following chelation treatment suggests a possible means for the solubilization of amyloid deposits. Expand
Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein.
A three-component band fitting is used to characterize the Raman amide I band of alpha-synuclein, phosvitin, alpha- casein, beta-casein, and the non-A beta component (NAC) of Alzheimer's plaque, demonstrating the ability of Raman spectroscopy to characterized the ensemble of secondary structures present in natively unfolded proteins. Expand
Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy
Formation of α-synuclein aggregates is proposed to be a crucial event in the pathogenesis of Parkinson's disease. Large soluble oligomeric species are observed as probable intermediates during fibrilExpand
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core
A homology model of the propionyl‐CoA carboxylase β‐subunit provides new insight into the propionic acidemia mechanism, its oligomeric structure and the molecular basis of mutations responsible for enzyme deficiency in Propionibacterium shermanii. Expand
Direct measurement of a pK(a) near neutrality for the catalytic cytosine in the genomic HDV ribozyme using Raman crystallography.
These studies provide the first direct physical measurement of a pKa near neutrality for a catalytic residue in a ribozyme and show that ribozymes, like their protein enzyme counterparts, can optimize the pKa of their side chains for proton transfer. Expand
Raman crystallography and other biochemical applications of Raman microscopy.
  • P. Carey
  • Chemistry, Medicine
  • Annual review of physical chemistry
  • 6 April 2006
Raman microscopy can provide detailed insights into the chemistry of the amyloid plaques associated with Alzheimer's disease and into the intermediates on the alpha-synuclein protein misfolding pathway implicated in Parkinson's disease. Expand
Secondary structure of alpha-synuclein oligomers: characterization by raman and atomic force microscopy.
The accumulation of spheroidal oligomers of increasing size but unchanged vibrational spectra during the fibrillization process suggests that a cooperative conformational change may contribute to the kinetic control of fibrilization. Expand
The mechanism of sunlight-mediated inactivation of Bacillus thuringiensis crystals.
The results concerning photodegradation support a photosensitization mechanism involving the presence of exogenous (and possibly endogenous) chromophores which create singlet oxygen species upon irradiation by light. Expand
Facile preparation and characterization of the toxin from Bacillus thuringiensis var. kurstaki.
The resistance of the toxin to most proteinases and its susceptibility to proteolysis by papain and Pronases indicates a compact multidomain structure. Expand