Ultraviolet
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            aman Spectrometry

Asher, Sanford A.

doi:10.1002/0470027320.s0408

Cited by 21 publications

(21 citation statements)

References 77 publications

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“…The effect was later named resonance Raman (RR) and a short review was recently given (63). The enhancement means that much more intensive spectra can be obtained and applied analytically but an inevitable problem is that samples get heated and often destroyed because of the absorption; however, certain samples can intentionally be moved, thereby avoiding decomposition (64)(65)(66). It has been known for long time that ascorbic acid absorbs in deep UV; the UV spectra of ascorbic acid/ascorbate in aqueous solution, for example, show π → π * absorption peaks at ∼243.5 and ∼265.5 nm (11) while being transparent in other ranges.…”

Section: Uv Resonance Raman Spectroscopymentioning

confidence: 99%

Investigation ofL(+)-Ascorbic acid with Raman spectroscopy in visible and UV light

Berg

2014

Applied Spectroscopy Reviews

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Section: Uv Resonance Raman Spectroscopymentioning

confidence: 99%

Investigation ofL(+)-Ascorbic acid with Raman spectroscopy in visible and UV light

Berg

2014

Applied Spectroscopy Reviews

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“…Utilization of UV irradiation at ;200 nm enables selective resonance enhancement of vibrational modes from amide chromophore (i.e., peptide bond), the building block of a polypeptide backbone. The technique, deep UV resonance Raman (DUVRR) spectroscopy, has been shown to be a powerful tool for structural characterization of proteins and polypeptides Asher 2001;Lednev et al 2005;Xu et al 2005;JiJi et al 2006). We have recently demonstrated that DUVRR spectroscopy can be used for probing structural evolution of an amyloidogenic protein at all stages of fibril formation .…”

mentioning

confidence: 99%

The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two‐state transition

Shashilov

Ermolenkov

et al. 2007

Protein Science

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Amyloid fibril depositions are associated with many neurodegenerative diseases as well as amyloidosis. The detailed molecular mechanism of fibrillation is still far from complete understanding. In our previous study of in vitro fibrillation of hen egg white lysozyme, an irreversible partially unfolded intermediate was characterized. A similarity of unfolding kinetics found for the secondary and tertiary structure of lysozyme using deep UV resonance Raman (DUVRR) and tryptophan fluorescence spectroscopy leads to a hypothesis that the unfolding might be a two-state transition. In this study, chemometric analysis, including abstract factor analysis (AFA), target factor analysis (TFA), evolving factor analysis (EFA), multivariate curve resolutionalternating least squares (ALS), and genetic algorithm, was employed to verify that only two principal components contribute to the DUVRR and fluorescence spectra of soluble fraction of lysozyme during the fibrillation process. However, a definite conclusion on the number of conformers cannot be made based solely on the above spectroscopic data although chemometric analysis suggested the existence of two principal components. Therefore, electrospray ionization mass spectrometry (ESI-MS) was also utilized to address the hypothesis. The protein ion charge state distribution (CSD) envelopes of the incubated lysozyme were well fitted with two principal components. Based on the above analysis, the partial unfolding of lysozyme during in vitro fibrillation was characterized quantitatively and proven to be a two-state transition. The combination of ESI-MS and Raman and fluorescence spectroscopies with advanced statistical analysis was demonstrated to be a powerful methodology for studying protein structural transformations.

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“…A 229 -nm excitation has been also used to probe histidine ligation via resonance enhancement of imidazole ring modes (181,208) . Deep UV excitation resonantly enhances Raman scattering from the amide chromophore, a building block of a polypeptide backbone (5,42,183) . Deep UV excitation resonantly enhances Raman scattering from the amide chromophore, a building block of a polypeptide backbone (5,42,183) .…”

Section: Ultraviolet Raman Spectroscopy For Characterizing Proteins Imentioning

confidence: 99%

Genetically Engineered Polypeptides as a Model of Intrinsically Disordered Fibrillogenic Proteins: Deep UV Resonance Raman Spectroscopic Study

Topilina

Sikirzhytski

Higashiya

et al. 2010

Instrumental Analysis of Intrinsically Disordered Proteins

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Protein misfolding plays an important role in many neurodegenerative diseases associated with proteinaceous aggregates having an extended cross -βsheet structure. Intrinsically disordered proteins (IDPs) can also be involved in the amyloid diseases. Genetic engineering facilitates examination of folding and fi brillation mechanisms by probing the infl uence of the primary polypeptide sequence on kinetic and equilibrium properties of the protein. This chapter focuses on the use of genetic engineering in the study of the mechanism of fi brillation of large biopolymers that are excellent models for intrinsically disordered proteins. The folding mechanism was probed using deep UV resonance Raman (DUVRR) spectroscopy, a novel method for acquisition of quantitative information on the peptide backbone conformation of large

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Ultraviolet R aman Spectrometry

Abstract: The sections in this article are Introduction Phenomenology Instrumentation Fundamental Applications Analytical Applications Biological Ultraviolet‐ R aman Studies Conclusions Acknowledgments

Cited by 21 publications

References 77 publications

Investigation ofL(+)-Ascorbic acid with Raman spectroscopy in visible and UV light

Investigation ofL(+)-Ascorbic acid with Raman spectroscopy in visible and UV light

The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two‐state transition

Genetically Engineered Polypeptides as a Model of Intrinsically Disordered Fibrillogenic Proteins: Deep UV Resonance Raman Spectroscopic Study

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