Raman tensors for the tryptophan side chain in proteins determined by polarized Raman microspectroscopy of oriented N-acetyl-l-tryptophan crystals

Tsuboi, Masamichi; Ueda, Toyotoshi; Ushizawa, Koichi; Ezaki, Yoshiko; Overman, Stacy A.; Thomas, George J.

doi:10.1016/0022-2860(95)09060-6

Cited by 31 publications

(38 citation statements)

References 21 publications

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“…For this purpose, we used the fourth derivative spectra whose resolution is superior with respect to the second-derivative spectra, allowing detecting also some weak component bands. The structural assignments of the band components were carried out on the basis of the literature [44][45][46][47].…”

Section: Raman Measurementsmentioning

confidence: 99%

Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes

Navarra

Tinti

Leone

et al. 2009

Journal of Inorganic Biochemistry

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Section: Raman Measurementsmentioning

confidence: 99%

Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes

Navarra

Tinti

Leone

et al. 2009

Journal of Inorganic Biochemistry

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“…24,51,52 Tsuboi and coworkers have developed a methodology to utilize the polarization anisotropy of nonresonance Raman scattering in determining Trp orientations in proteins and peptides. [53][54][55] Polarized Raman spectroscopy is a promising tool for detailed structural analysis of oriented protein molecules.…”

Section: To Nnј-bis(2-(3-indolyl)ethyl)-413-diaza-18-crown-6mentioning

confidence: 99%

Raman structural markers of tryptophan and histidine side chains in proteins

2003

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The Raman spectrum of a protein contains a wealth of information on the structure and interaction of the protein. To extract the structural information from the Raman spectrum, it is necessary to identify and interpret the marker bands that reflect the structure and interaction in the protein. Recently, new Raman structural markers have been proposed for the tryptophan and histidine side chains by examining the spectra-structure correlations of model compounds. Raman structural markers are now available for the conformation, hydrogen bonding, hydrophobic interaction, and cation-pi interaction of the indole ring of Trp. For His, protonation, tautomerism, and metal coordination of the imidazole ring can be studied by using Raman markers. The high-resolution X-ray crystal structures of proteins provide the basis for testing and modifying the Raman structural markers of Trp and His. The structures derived from Raman spectra are generally consistent with the X-ray crystal structures, giving support for the applicability of most Raman structural makers. Possible modifications and limitations to some marker bands are also discussed.

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“…1c. 8) To determine the Raman tensor of the 1560 cm −1 Raman band of tryptophan the following strategy was employed. Let us assume that the principal axes are those designated Trp1 in Fig.…”

Section: Methods For Raman Tensor Determinationsmentioning

confidence: 99%

“…In each orientation the incident and scattered electric vectors are parallel to one of the crystallographic axes, as defined above. 8) …”

Section: Methods For Raman Tensor Determinationsmentioning

confidence: 99%

Raman Tensors and their application in structural studies of biological systems

Tsuboi

Benevides

Thomas

2009

Proc. Jpn. Acad., Ser. B

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The Raman scattering of a molecule is generated by interactions of its electrons with incident light. The electric vector of the Raman scattered light is related to the electric vector of the incident light through a characteristic Raman tensor. A unique Raman tensor exists for each Raman-active molecular vibrational mode. In the case of biologically important macromolecules Raman tensors have been determined for a few hundred vibrational Raman bands. These include proteins and their amino acid constituents, as well as nucleic acids (DNA and RNA) and their nucleotide constituents. In this review Raman tensors for 39 representative vibrational Raman bands of biological molecules are considered. We present details of the Raman tensor determinations and discuss their application in structural studies of filamentous bacteriophages (fd, Pf1, Pf3 and PH75), fowl feather rachis and eyespots of the protists, Chlamydomonas and Euglena.

show abstract

Raman tensors for the tryptophan side chain in proteins determined by polarized Raman microspectroscopy of oriented N-acetyl-l-tryptophan crystals

Cited by 31 publications

References 21 publications

Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes

Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes

Raman structural markers of tryptophan and histidine side chains in proteins

Raman Tensors and their application in structural studies of biological systems

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