Publications by authors named "J S Handen"
UV resonance Raman (UVRR) spectroscopy is a powerful tool for investigating the structure of biological molecules, such as proteins. Numerous UVRR spectroscopic markers that provide information on the structure and environment of the protein backbone and of amino acid side chains have recently been discovered. Combining these UVRR markers with hydrogen-deuterium exchange and advanced statistics is a powerful tool for studying protein systems, including the structure and formation mechanism of protein aggregates and amyloid fibrils.
View Article and Find Full Text PDFDeep UV Resonance Raman Spectroscopy for Characterizing Amyloid Aggregation.
Methods Mol Biol
July 2016
Article Synopsis
- Deep UV resonance Raman spectroscopy is an effective method for analyzing protein fibrils, overcoming challenges like low solubility and noncrystalline arrangements.
- This technique allows for selective enhancement of various chromophores in protein fibrils, providing insights into their structure and formation mechanisms.
- Advanced methods such as hydrogen-deuterium exchange and chemometrics can further detail the fibril core structure and protein interactions during fibril formation.
Article Synopsis
- The first measurement of vibrational circular dichroism (VCD) spectra for microcrystals of fibril-forming peptides, specifically human islet amyloid polypeptide (IAPP), was conducted.
- The study compared the VCD spectra of microcrystals and fibrils from the same peptide to gather insights into their structural characteristics and supramolecular chirality.
- It was found that enhanced VCD in these structures does not depend on the twisting of multiple filaments, which is a characteristic of fibrils but not microcrystals.