Measurement of cross sections for two-photon absorption of aromatic amino acids

Meshalkin, Yu. P.; Alfimov, E. E.; Groshev, D. E.; Makukha, Vladimir K.

doi:10.1007/bf02606599

Cited by 4 publications

(4 citation statements)

References 3 publications

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“…Among all aromatic amino acids, tryptophan (Trp) exhibits the largest UV absorption cross section 1 and, in solution, exhibits the highest fluorescence quantum yield. 2 This residue, therefore, represents a benchmark photoactive building block of proteins.…”

Section: Introductionmentioning

confidence: 99%

“…structural motifs of the two lowest-energy conformers A and B are(1) alignment of an amine N-H bond toward the acid group's C=O bond, rather than the O-H bond, and (2) positioning of the protonated-amine N-H + toward the middle of the face of the indole moiety, rather than toward the end of the pyrrole ring. All other, higher-energy conformers lack one or both of these interactions, suggesting that these two unique factors are the source of the stability of the dominant isomers.…”

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confidence: 98%

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Vibrational Signatures of Conformer-Specific Intramolecular Interactions in Protonated Tryptophan

et al. 2016

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Because of both experimental and computational challenges, protonated tryptophan has remained the last aromatic amino acid for which the intrinsic structures of low-energy conformers have not been unambiguously solved. The IR-IR-UV hole-burning spectroscopy technique has been applied to overcome the limitations of the commonly used IR-UV double resonance technique and to measure conformer-specific vibrational spectra of TrpH(+), cooled to T = 10 K. Anharmonic ab initio vibrational spectroscopy simulations unambiguously assign the dominant conformers to the two lowest-energy geometries from benchmark coupled-cluster structure computations. The match between experimental and ab initio spectra provides an unbiased validation of the calculated structures of the two experimentally observed conformers of this benchmark ion. Furthermore, the vibrational spectra provide conformer-specific signatures of the stabilizing interactions, including hydrogen bonding and an intramolecular cation-π interaction.

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Section: Introductionmentioning

confidence: 99%

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confidence: 98%

Vibrational Signatures of Conformer-Specific Intramolecular Interactions in Protonated Tryptophan

et al. 2016

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“…The excitation beam of 532 nm matched to the resonance condition because of the third term in Equation . The cross‐section for the two‐photon absorption of the 532‐nm excitation aromatic amino acids was in the range of 10 −51 –10 −52 cm 4 s photon −1 mol −1 and large enough to be determined …”

Section: Resultsmentioning

confidence: 99%

The 532‐nm‐excited hyper‐Raman spectroscopy of globular protein and aromatic amino acids

Wen

Hiramatsu

2019

J Raman Spectroscopy

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Hyper‐Raman (HR) spectroscopy reveals unique information about molecular structures, because of its different selection rule, compared with that of the infrared (IR) and Raman spectroscopy. The application of HR spectroscopy on biomolecules' research has been expected for a long time. Herein, we report the HR spectra of the amino acids tryptophan (Trp), tyrosine (Tyr), histidine, and bovine serum albumin (BSA) in aqueous solution, obtained at an excitation wavelength of 532 nm. The HR bands of BSA were mostly assigned to those of the aromatic amino acids. The predominance of the aromatic amino acids was explained by considering the resonance effect of the excitation beam to the electronic absorption around 266 nm, the double frequency of 532 nm (e.g. La of Trp, Lb of Tyr). Besides the Raman bands observed in the 266‐nm‐excited ultraviolet resonance Raman spectrum, some of the IR‐active bands of Tyr were also detected. Hence, the HR spectroscopy serves as a new tool toward the investigation of proteins as well as of biomolecules and more complicated biological structures with the 532‐nm excitation.

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“…As seen in the literature, atomic cross sections and total dissociative electron attachment cross sections have been studied for the amino acids, glycine, alanine, proline, phenylalanine, and tryptophan, at energies below the first ionization energy by Scheer et al [ 7 ]. Also, cross sections have been measured for two-photon absorption of aromatic amino acids by Meshalkin et al [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Photon Atomic Parameters of Nonessential Amino Acids for Radiotherapy and Diagnostics

Bursalıoğlu

İçelli

Balkan

et al. 2014

Journal of Amino Acids

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The total mass attenuation coefficients (μ t) (cm2/g) and atomic, molecular, and electronic effective cross sections have been calculated for nonessential amino acids that contain H, C, N, and O such as tyrosine, aspartate, glutamine, alanine, asparagine, aspartic acid, cysteine, and glycine in the wide energy region 0.015–15 MeV. The variations with energy of total mass attenuation coefficients and atomic, molecular, and electronic cross sections are shown for all photon interactions.

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Measurement of cross sections for two-photon absorption of aromatic amino acids

Cited by 4 publications

References 3 publications

Vibrational Signatures of Conformer-Specific Intramolecular Interactions in Protonated Tryptophan

Vibrational Signatures of Conformer-Specific Intramolecular Interactions in Protonated Tryptophan

The 532‐nm‐excited hyper‐Raman spectroscopy of globular protein and aromatic amino acids

Photon Atomic Parameters of Nonessential Amino Acids for Radiotherapy and Diagnostics

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