The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics
Open accessAbstract
A study was conducted to demonstrate ultraviolet resonance Raman (UVRR) investigations of peptide and protein structure and dynamics. The tuning of the excitation wavelengths allowed the probing of different chromophoric segments of a macromolecule. Another advantage of deep UV Raman measurements was that there was no interference from molecular relaxed fluorescence, as those chromophores that had their first transition below 260 nm were highly flexible and possessed small fluorescence quantum yields. UVRR was also used in pump-probe measurements to give kinetic information on fast biological processes. It was a powerful technique for studying static protein structure and for studying protein dynamics, such as in protein folding. The rapid development of UVRR was aided by the latest advancements in lasers, optics, and detectors.
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An Information-Maximization Approach to Blind Separation and Blind Deconvolution
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From Levinthal to pathways to funnels
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Two‐Dimensional Correlation Spectroscopy – Applications in Vibrational and Optical Spectroscopy
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Metadata
- Authors
- Oladepo, S. A., Xiong, K., Hong, Z., Asher, S. A., Handen, J., & Lednev, I. K.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-02-15
- Volume
- 112
- Issue
- 5
- Pages
- 2604-2628
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2053043974
- Cited by
- 214
- References
- 5
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- green
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