Paper
2 May 1997 In-situ investigation of protein and DNA structure using UVRRS
L. Shane Greek, H. Georg Schulze, Michael W. Blades, Charles A. Haynes, Robin F. B. Turner
Author Affiliations +
Abstract
Ultraviolet resonance Raman spectroscopy (UVRRS) has the potential to become a sensitive, specific, versatile bioanalytical and biophysical technique for routine investigations of proteins, DNA, and their monomeric components, as well as a variety smaller, physiologically important aromatic molecules. The transition of UVRRS from a complex, specialized spectroscopic method to a common laboratory assay depends upon several developments, including a robust sample introduction method permitting routine, in situ analysis in standard laboratory environments. To this end, we recently reported the first fiber-optic probes suitable for deep-UV pulsed laser UVRRS. In this paper, we extend this work by demonstrating the applicability of such probes to studies of biochemical relevance, including investigations of the resonance enhancement of phosphotyrosine, thermal denaturation of RNase T1, and specific and non-specific protein binding. The advantages and disadvantages of the probes are discussed with reference to sample conditions and probe design considerations.
© (1997) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
L. Shane Greek, H. Georg Schulze, Michael W. Blades, Charles A. Haynes, and Robin F. B. Turner "In-situ investigation of protein and DNA structure using UVRRS", Proc. SPIE 2982, Optical Diagnostics of Biological Fluids and Advanced Techniques in Analytical Cytology, (2 May 1997); https://doi.org/10.1117/12.273609
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Cited by 3 scholarly publications.
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KEYWORDS
Proteins

Fiber optics

Raman spectroscopy

Silica

Resonance enhancement

Chlorine

Spectroscopy

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