Raman Spectra of Crystalline Lysozyme, Pepsin, and Alpha Chymotrypsin

Tobin, Marvin C.

doi:10.1126/science.161.3836.68

Cited by 59 publications

(26 citation statements)

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“…[4][5][6][7][8][9][10][11][12] Variations in the environment of molecular components of materials and tissues are reflected in shifts in absorbance band intensities and positions in vibrational spectra. [4][5][6][7][8][9][10][11][12] Variations in the environment of molecular components of materials and tissues are reflected in shifts in absorbance band intensities and positions in vibrational spectra.…”

Section: Introductionmentioning

confidence: 99%

Infrared and Raman Microscopy and Imaging of Biomaterials

Kavukcuoglu

Pleshko

2011

Comprehensive Biomaterials

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Section: Introductionmentioning

confidence: 99%

Infrared and Raman Microscopy and Imaging of Biomaterials

Kavukcuoglu

Pleshko

2011

Comprehensive Biomaterials

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“…In the past few years the technique of laser Raman spectroscopy has been used with considerable success to obtain the Raman active vibrations of several proteins (1)(2)(3)(4). However, if one examines the published spectra, it is apparent that it has been impossible in the past to obtain the Raman bands in proteins that lie below 150 cm-'.…”

mentioning

confidence: 99%

Conformationally Dependent Low-Frequency Motions of Proteins by Laser Raman Spectroscopy

Brown

Erfurth

Small

et al. 1972

Proc. Natl. Acad. Sci. U.S.A.

178

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Low-frequency Raman bands (lower than 50 cm-') exist in certain proteins. They are dependent upon the conformation of the protein molecule, but are relatively independent of the form of the sample, i.e., whether it is a film or a crystal.Low-frequency Raman spectra were obtained from samples of a-chymotrypsin that had been prepared in several ways. A peak at about 29 cm-' was found for all samples except the one that had been denatured with sodium dodecyl sulfate. Such low frequency motions must arise from vibrations that involve all, or very large portions, of the protein molecule.In the past few years the technique of laser Raman spectroscopy has been used with considerable success to obtain the Raman active vibrations of several proteins (1-4). However, if one examines the published spectra, it is apparent that it has been impossible in the past to obtain the Raman bands in proteins that lie below 150 cm-'. The reason for this is that the scattering due to the Rayleigh component is too large for a double-grating monochromator to discriminate against. Recently, in this laboratory, we have shown how to obtain Raman spectra only a few wave numbers from the exciting line on synthetic polymers, such as polyethylene and poly-i-alanine, by the iodine filter technique (5-7) and a Spex double-grating monochromator. More recently, we have also found it possible to obtain these low frequency bands using a Cary triple-grating monochromator. For the work reported here, we have used both of these instruments and have obtained equivalent results on each. This has been of the greatest help in elimination of the possibility of experimental artifacts. From our work with these instruments it is possible to show, for the first time, that definite low-frequency motions exist in many common proteins and that these vibrations appear to be sensitive to the conformation of the protein. As we will discuss below, such low-frequency motions must arise from vibrations that involve either all or very large portions of the protein molecule. Thus, it appears from our measurements that large portions of the protein molecule are constantly undergoing a coherent periodic vibration. The existence of such vibrations is of considerable interest even though the exact assignment of the motion is not possible at present.Figs. la and b show the low-frequency Raman spectra of samples of a-chymotrypsin that were prepared in several ways. In every case, except the sample that had been denatured with SDS, a pronounced peak at about 29 cm-' is found. It is apparent that there is some splitting of the peak in the single crystal and also some slight change in the shape of the peak with deuteration and acylation. However, upon denaturation with SDS the peak at 29 cm-' vanishes. Rather intense Raman scattering throughout the region of 20-150 cm-' is observed on the denatured material, but it is broad and structureless-a fact that probably reflects the decrease in the order of the protein conformation.The fact that this low-frequency band is dependent ...

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“…The first laser Raman spectra of proteins were recorded by Tobin in 1968 [62]. Strekas and Spiro [63] and Brunner and colleagues [64] first reported Raman spectra of Hb in 1972.…”

Section: Band Assignment In Heme-based Moleculesmentioning

confidence: 98%

Resonance Raman spectroscopy in malaria research

Wood¹

2006

Expert Review of Proteomics

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In recent years, the field of Raman spectroscopy has witnessed a surge in technological development, with the incorporation of ultrasensitive, charge-coupled devices, improved laser sources and precision Rayleigh-filter systems. This has led to the development of sensitive confocal micro-Raman spectrometers and imaging spectrometers that are capable of obtaining high spatial-resolution spectra and images of subcellular components within single living cells. This review reports on the application of resonance micro-Raman spectroscopy to the study of malaria pigment (hemozoin), a by-product of hemoglobin catabolization by the malaria parasite, which is an important target site for antimalarial drugs. The review aims to briefly describe recent studies on the application of this technology, elucidate molecular and electronic properties of the malaria pigment and its synthetic analog beta-hematin, provide insight into the mechanism of hemozoin formation within the food vacuole of the parasite, and comment on developing strategies for using this technology in drug-screening protocols.

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Raman Spectra of Crystalline Lysozyme, Pepsin, and Alpha Chymotrypsin

Cited by 59 publications

References 4 publications

Infrared and Raman Microscopy and Imaging of Biomaterials

Infrared and Raman Microscopy and Imaging of Biomaterials

Conformationally Dependent Low-Frequency Motions of Proteins by Laser Raman Spectroscopy

Resonance Raman spectroscopy in malaria research

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