Comparison of the UV Resonance Raman Spectra of Bacteria, Bacterial Cell Walls, and Ribosomes Excited in the Deep UV
- 1 January 1993
- journal article
- Published by SAGE Publications in Applied Spectroscopy
- Vol. 47 (1) , 38-43
- https://doi.org/10.1366/0003702934048505
Abstract
Resonance Raman spectra have been obtained with 218-nm excitation for Escherichia coli and Staphylococcus epidermidis. Large intensity differences seen in the tryptophan-associated 1556-cm−1 peak appear to be strongly related to Gram type. Unlike E. coli, S. epidermidis possess a very intense peak at 1658 cm−1 which varies in intensity with cultural conditions. Spectra excited from E. coli and Enterobacter aerogenes with 200-nm light show peaks which strongly reflect nucleic acid composition, unlike spectra excited at 218 nm. Purified, separated ribosomes of E. coli produce spectra which are dominated by nucleic acid vibrations when excited at 242 nm, but have peaks belonging nearly exclusively to protein aromatic amino acids when excited at 222 nm. The relative weakness of bacterial RNA modes excited at 222 nm from whole cells and ribosomes is attributed to nucleic acid hypochromism.Keywords
This publication has 29 references indexed in Scilit:
- UV Resonance Raman Studies of BacteriaApplied Spectroscopy Reviews, 1992
- UV Resonance Raman Spectra of Bacillus SporesApplied Spectroscopy, 1992
- Resonance Raman Spectra of Aqueous Pollen Suspensions with 222.5–242.4-nm Pulsed Laser ExcitationApplied Spectroscopy, 1991
- UV resonance Raman spectra of bacteria, bacterial spores, protoplasts and calcium dipicolinateJournal of Microbiological Methods, 1990
- Ultra-Violet Resonance Raman Spectra of Live Cyanobacteria with 222.5–251.0 nm Pulsed Laser ExcitationApplied Spectroscopy, 1989
- Ultraviolet Resonance Raman Spectra of Escherichia Coli with 222.5–251.0 nm Pulsed Laser ExcitationApplied Spectroscopy, 1988
- An Ultraviolet (242 nm Excitation) Resonance Raman Study of Live Bacteria and Bacterial ComponentsApplied Spectroscopy, 1987
- Ultraviolet Raman hypochromism of the tropomyosin amide modes: a new method for estimating .alpha.-helical content in proteinsJournal of the American Chemical Society, 1986
- Poly(dA-dT) complexes with histone H1 and pancreatic ribonuclease: Specific base recognition evidenced by ultraviolet resonance Raman spectroscopyBiopolymers, 1982
- Ultraviolet Raman spectroscopy of polyribouridylic acid: Excitation profile of the hypochromism induced by order-disorder transitionBiopolymers, 1980