Disease relevance of Spectrum Analysis, Raman

• Examination of a number of site-directed mutants of E. coli CcmE by resonance Raman spectroscopy has identified ligands of the heme iron and provided insight into the initial steps of heme binding by CcmE before it binds the heme covalently [1].
• An investigation of hydrogenase I and hydrogenase II from Clostridium pasteurianum by resonance Raman spectroscopy. Evidence for a [2Fe-2S] cluster in hydrogenase I [2].
• The Pr --> Pfr phototransformation of the bacteriophytochrome Agp1 from Agrobacterium tumefaciens and the structures of the biliverdin chromophore in the parent states and the cryogenically trapped intermediate Meta-R(C) were investigated with resonance Raman spectroscopy and flash photolysis [3].
• The viral shell has been investigated using time and temperature resolved Raman and ultraviolet-resonance Raman spectroscopy to reveal novel features of the capsid structure and its pathway of assembly from P3 subunits [4].
• Raman spectroscopy of filamentous bacteriophage Ff (fd, M13, f1) incorporating specifically-deuterated alanine and tryptophan side chains. Assignments and structural interpretation [5].

Psychiatry related information on Spectrum Analysis, Raman

• Near-infrared Raman spectroscopy can be a new technique for physical evaluations, allowing the measurement of lactic acid concentrations, in blood or muscles, during the physical activity in a transcutaneous non-invasive way [6].

High impact information on Spectrum Analysis, Raman

• The formation of vibrationally excited heme upon photodissociation of carbonmonoxy myoglobin and its subsequent vibrational energy relaxation was monitored by picosecond anti-Stokes resonance Raman spectroscopy [7].
• Resonance Raman spectroscopy has been used to identify both C-O stretching and metal-CO stretching vibrations of the carbon monoxide adduct of the enzyme [8].
• Pulse-probe transient Raman spectroscopy, with probe excitation at 230 nanometers, reveals changes in signals arising from tyrosine and tryptophan residues of the hemoglobin molecule as it moves from the relaxed (R) to the tense (T) state after photodeligation [9].
• To assess possible consequences of electric fields on the redox processes of cytochrome c, the protein can be immobilized to self-assembled monolayers on electrodes and studied by surface-enhanced resonance Raman spectroscopy [10].
• Electron-transfer processes of cytochrome C at interfaces. New insights by surface-enhanced resonance Raman spectroscopy [10].

Chemical compound and disease context of Spectrum Analysis, Raman

• N-terminal domain of the bacteriophage lambda repressor: investigation of secondary structure and tyrosine hydrogen bonding in wild-type and mutant sequences by Raman spectroscopy [11].
• Active site properties of the 3C proteinase from hepatitis A virus (a hybrid cysteine/serine protease) probed by Raman spectroscopy [12].
• Reaction intermediates in dioxygen reduction by the E. coli cytochrome bo-type ubiquinol oxidase were studied by time-resolved resonance Raman spectroscopy using the artificial cardiovascular system [13].
• At each hemorrhage and resuscitation interval, Raman spectroscopy was performed and corresponding arterial and central venous blood gas and lactate measurements were made [14].
• We also show that the MP Raman spectroscopy technology has potential as a novel, highly specific method for rapid screening of carotenoid antioxidant levels in large populations at risk for vision loss from age-related macular degeneration, the leading cause of blindness of the elderly in the developed world [15].

Biological context of Spectrum Analysis, Raman

• Resonance Raman spectroscopy and ligand association/dissociation kinetic measurements, along with mutagenesis studies, reveal that the stabilization of the bound oxygen is achieved through a tyrosine at the B10 position in the distal pocket of the heme with a conformation that is unique among the globins [16].
• Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics [17].
• Solution conformations and interactions of alpha and beta subunits of the Oxytricha nova telomere binding protein: investigation by Raman spectroscopy [18].
• Interactions between telomeric DNA and the alpha subunit of the heterodimeric telomere binding protein of Oxytricha nova have been probed by Raman spectroscopy, CD spectroscopy, and nondenaturing gel electrophoresis [19].
• We have studied the binding nature of an aromatic aldehyde to the catalytic site of liver alcohol dehydrogenase from horse (LADH) using preresonance Raman spectroscopy [20].

Anatomical context of Spectrum Analysis, Raman

• We use time-resolved coherent Raman spectroscopy to obtain molecule-specific signals from dipicolinic acid (DPA), which is a marker molecule for bacterial spores [21].
• The derivatives of calf thymus DNA in which n-butylamine is covalently attached as described in the preceding paper in this series [Chen, C. Y., Pheiffer, B. H., Zimmerman, S. B., & Hanlon, S. (1983) Biochemistry (preceding paper in this issue)] were examined by Raman spectroscopy [22].
• The effects of calcium ions on mixed membranes of dimyristoylphosphatidic acid (DMPA) and dimyristoylphosphatidylcholine (DMPC) with either the PA or the PC component deuterated have been studied by Raman spectroscopy [23].
• The paper describes the first in situ detection of glutamate in single nerve terminals (synaptosomes), which is achieved by using laser trapping Raman spectroscopy [24].
• Glucose determination in human aqueous humor with Raman spectroscopy [25].

Associations of Spectrum Analysis, Raman with chemical compounds

• Splittings related to the stretching vibration of bound dioxygen in hemoproteins have been detected by resonance Raman spectroscopy [26].
• Resonance Raman spectroscopy provides evidence that bR570 is protonated, but these results have been questioned on the basis of theoretical and experimental grounds [27].
• Visible and UV coherent Raman spectroscopy of dipicolinic acid [21].
• UV resonance Raman spectroscopy was used to detect and estimate the frequency of the unfavored imino tautomer of the transition mutagen 5-hydroxy-2'-deoxycytidine (HO5dCyt) in its anionic form [28].
• The binding of distamycin and netropsin to duplex DNA has been studied by Raman spectroscopy [29].

Gene context of Spectrum Analysis, Raman

• Resonance Raman spectroscopy of NCB5OR presents typical signatures of a six-coordinate low-spin heme similar to those found in other cytochrome b5 proteins [30].
• We have used resonance Raman spectroscopy to characterize the heme environment of purified recombinant human indoleamine 2,3-dioxygenase (hIDO) [31].
• To characterize the structure/function relationships of this new heme protein, we have used resonance Raman spectroscopy to determine the structure of the heme environment in Ngb from mice [32].
• Fourier-transform Raman spectroscopy revealed unexpected differences between NR and bacteriorhodopsin in the configuration of the retinal chromophore, which may contribute to the less effective reprotonation switch of NR [33].
• Rapid-flow resonance Raman spectroscopy of photolabile molecules: rhodopsin and isorhodopsin [34].

Analytical, diagnostic and therapeutic context of Spectrum Analysis, Raman

• Laser Raman spectroscopy and circular dichroism studies of the peptide hormones mesotocin, vasotocin, lysine vasopressin, and arginine vasopressin. Conformational analysis [35].
• Shock-recovery experiments have been conducted on 6H polytype silicon carbide to 135 GPa and post-shock samples have been analyzed by Raman spectroscopy, x-ray diffraction, and electron microscopy [36].
• Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography [37].
• The catalyst precursors were also characterized in the solid state by thermogravimetric analysis, FTIR, and Raman spectroscopy, and MAS NMR ((13)C, (119)Sn) spectroscopy [38].
• Isolated complexes of apolipoprotein A-I (apoA-I), the major apoprotein of human plasma high-density lipoproteins, and dimyristoylphosphatidylcholine (DMPC) have been prepared and studied by differential scanning calorimetry (DSC) and Raman spectroscopy [39].

References