ArticleThe journal of physical chemistry. B2019
UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide.
Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Deep UV Resonance Raman Spectroscopy: Applications to Membrane Proteins and Peptides.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Photocontrol of the β-Hairpin Polypeptide Structure through an Optimized Azobenzene-Based Amino Acid Analogue.Journal of the American Chemical Society · 2024Article
- pH-controlled stacking direction of the β-strands in peptide fibrils.Scientific reports · 2020Article
- Polyglutamine Solution-State Structural Propensity Is Repeat Length Dependent.The journal of physical chemistry. B · 2019Article
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Authors and funding
3 authors.
Funding
Abstract
Fibrillization of polyglutamine (polyQ) tracts in proteins is implicated in at least 10 neurodegenerative diseases. This generates great interest in the structure and the aggregation mechanism(s) of polyQ peptides. The fibrillization of polyQ is thought to result from the peptide's insolubility in aqueous solutions; longer polyQ tracts show decreased aqueous solution solubility, which is thought to lead to faster fibrillization kinetics. However, few studies have characterized the structure(s) of polyQ peptides with low solubility. In the work here, we use UV resonance Raman spectroscopy to examine the secondary structures, backbone hydrogen bonding, and side chain hydrogen bonding for a variety of solution-state, solid, and fibril forms of D
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