ArticleThe journal of physical chemistry. B2015
Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.
Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Lighting the Path: Raman Spectroscopy's Journey Through the Microbial Maze.Molecules (Basel, Switzerland) · 2024Article
- Toward determining amyloid fibril structures using experimental constraints from Raman spectroscopy.The Journal of chemical physics · 2023Article
- Quinine copolymer reporters promote efficient intracellular DNA delivery and illuminate a protein-induced unpackaging mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Polyglutamine Solution-State Structural Propensity Is Repeat Length Dependent.The journal of physical chemistry. B · 2019Article
- UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide.The journal of physical chemistry. B · 2019Article
- Ultraviolet Resonance Raman Spectroscopic Markers for Protein Structure and Dynamics.Trends in analytical chemistry : TRAC · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
We identified vibrational spectral marker bands that sensitively report on the side chain structures of glutamine (Gln) and asparagine (Asn). Density functional theory (DFT) calculations indicate that the Amide III(P) (AmIII(P)) vibrations of Gln and Asn depend cosinusoidally on their side chain OCCC dihedral angles (the χ3 and χ2 angles of Gln and Asn, respectively). We use UV resonance Raman (UVRR) and visible Raman spectroscopy to experimentally correlate the AmIII(P) Raman band frequency to the primary amide OCCC dihedral angle. The AmIII(P) structural sensitivity derives from the Gln (Asn) Cβ-Cγ (Cα-Cβ) stretching component of the vibration. The Cβ-Cγ (Cα-Cβ) bond length inversely correlates with the AmIII(P) band frequency. As the Cβ-Cγ (Cα-Cβ) bond length decreases, its stretching force constant increases, which results in an upshift in the AmIII(P) frequency. The Cβ-Cγ (Cα-Cβ) bond length dependence on the χ3 (χ2) dihedral angle results from hyperconjugation between the Cδ═Oϵ (Cγ═Oδ) π* and Cβ-Cγ (Cα-Cβ) σ orbitals. Using a Protein Data Bank library, we show that the χ3 and χ2 dihedral angles of Gln and Asn depend on the peptide backbone Ramachandran angles. We demonstrate that the inhomogeneously broadened AmIII(P) band line shapes can be used to calculate the χ3 and χ2 angle distributions of peptides. The spectral correlations determined in this study enable important new insights into protein structure in solution, and in Gln- and Asn-rich amyloid-like fibrils and prions.
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