Structures and Dynamics of Proteins Probed by UV Resonance Raman Spectroscopy

Leigh, Brian S.; Schlamadinger, Diana E.; Kim, Judy E.

doi:10.1002/9781118354698.ch9

Cited by 2 publications

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“…Off-resonance Raman studies of tryptophan have played a critical role in the interpretation of UVRR spectra. − These and other off-resonance studies have correlated Raman peaks to molecular details of tryptophan, such as hydrogen-bonding strength, microenvironment, structure, and cation−π interactions. UVRR reveals analogous insights, including local hydrophobicity, strength of indole NH hydrogen bond, and torsional angle, χ 2,1 , about the C-2–C-3–Cβ–Cα linkage. − The wealth of vibrational information makes tryptophan an ideal probe in biophysical studies.…”

Section: Introductionmentioning

confidence: 99%

Raman and Quantum Yield Studies of Trp48-d₅ in Azurin: Closed-Shell and Neutral Radical Species

et al. 2019

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Isotopologues are valuable vibrational probes that shift features in a vibrational spectrum while preserving the electronic structure of the molecule. We report the vibrational and electronic spectra of perdeuterated tryptophan in solution (l-Trp-d 5), as Trp48-d 5 in azurin, and as the photogenerated neutral tryptophan radical, Trp48-d 5 •, in azurin. The UV resonance Raman bands of the perdeuterated closed-shell tryptophan in solution and in azurin are lower in frequency relative to the protiated counterpart. The observed decrease in frequencies of l-Trp-d 5 bands relative to l-Trp-h 5 enables the analysis of vibrational markers of other amino acids, e.g., phenylalanine, that overlap with some modes of l-Trp-h 5. The Raman intensities vary between l-Trp-d 5 and l-Trp-h 5; these differences likely reflect modifications in normal mode composition upon perdeuteration. Analysis of the W3, W6, and W17 modes suggests that the W3 mode retains its utility as a conformational marker; however, the H-bond markers W6 and W17 appear to be less sensitive upon perdeuteration. The neutral tryptophan radical, Trp48-d 5 •, was generated in azurin with a slightly lower radical quantum yield than for Trp48-h 5 •. The visible resonance Raman spectrum of Trp48-d 5 • is different from that of Trp48-h 5 •, especially in terms of relative intensities, and all assignable peaks decreased in frequency upon perdeuteration. The absorption and emission spectra of the perdeuterated closed-shell and radical species exhibited hypsochromic shifts of less than 1 nm relative to the protiated species. The data presented here indicate that l-Trp-d 5 is a valuable probe of vibrational structure, with minimal modification of photoreactivity and photophysics compared to l-Trp-h 5.

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Section: Introductionmentioning

confidence: 99%

Raman and Quantum Yield Studies of Trp48-d₅ in Azurin: Closed-Shell and Neutral Radical Species

et al. 2019

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Visible and UV resonance Raman spectroscopy of the peroxide-based explosive HMTD and its photoproducts

2016

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Structures and Dynamics of Proteins Probed by UV Resonance Raman Spectroscopy

Cited by 2 publications

References 100 publications

Raman and Quantum Yield Studies of Trp48-d₅ in Azurin: Closed-Shell and Neutral Radical Species

Raman and Quantum Yield Studies of Trp48-d₅ in Azurin: Closed-Shell and Neutral Radical Species

Visible and UV resonance Raman spectroscopy of the peroxide-based explosive HMTD and its photoproducts

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Structures and Dynamics of Proteins Probed by UV Resonance Raman Spectroscopy

Cited by 2 publications

References 100 publications

Raman and Quantum Yield Studies of Trp48-d5 in Azurin: Closed-Shell and Neutral Radical Species

Raman and Quantum Yield Studies of Trp48-d5 in Azurin: Closed-Shell and Neutral Radical Species

Visible and UV resonance Raman spectroscopy of the peroxide-based explosive HMTD and its photoproducts

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Product

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Raman and Quantum Yield Studies of Trp48-d₅ in Azurin: Closed-Shell and Neutral Radical Species

Raman and Quantum Yield Studies of Trp48-d₅ in Azurin: Closed-Shell and Neutral Radical Species