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Tris spectrum

Fig. 9.25 If the leucine side chain interconverts rapidly between too conprmations then the NMR spectrum will he an average of them. With a traditional refinement this leads to a structure that sirmltaiieausly tries to satisfy all restraints and is at the top of the energy barrier between the two minima. Fig. 9.25 If the leucine side chain interconverts rapidly between too conprmations then the NMR spectrum will he an average of them. With a traditional refinement this leads to a structure that sirmltaiieausly tries to satisfy all restraints and is at the top of the energy barrier between the two minima.
For example, a metastable peak appeared at 147.9 mass units in a mass spectrum with prominent peaks at 65, 91, 92, 107, 108, 155, 172, and 200 mass units. Try all possible combinations in the above expression. The fit is given by... [Pg.814]

In addition to low volatility, the chosen liquid should be a good all-around solvent. Since no one liquid is likely to have the required solvency characteristics, several are in use (Table 4.1). If a mass spectmm cannot be obtained in one solvent, it is useful to try one or more others before deciding that an FAB spectrum cannot be obtained. [Pg.21]

Once a mass spectrum from an eluting component has been acquired, the next step is to try to identify the component either through the skill of the mass spectroscopist or by resorting to a library search. Most modem GC/MS systems with an attached data station include a large library of spectra from known compounds (e.g., the NIST library). There may be as many as 50,000 to 60,000 stored spectra covering most of the known simple volatile compounds likely to be met in analytical work. Using special search routines under the control of the computer, one can examine... [Pg.257]

However, the two levels may become obvious if the instrument operator tries, for example, to conduct a library search while the computer is trying to acquire input from another mass spectrum the library search has to wait. Acquiring the data is a foreground task. Other functions such as library searching are background tasks. [Pg.421]

Although extremelv useful, tracer experiments require considerable capital expenditures and personnel. In addition to the difficulties and uncertainty in making estimates of various parameters, especially cr, one of the fficulties in interpreting tracer studies is relating the atmospheric conditions under which the study was conducted to the entire spectrum of atmospheric conditions. For example, trying to interpret a series of tracer... [Pg.314]

In specialized cases, a treatment known as canonization sometimes is tried to improve the amount of molecular (chemical) information made available. If Ag or Na are deliberately introduced into the sample, they will ofren combine with the molecular species present to create Ag or Na molecular ions. These ions are more stable to fragmentation than the bare molecular ions, and can therefore be observed more easily in the mass spectrum. The identification of parent ion peaks in this manner aids in detailed chemical identification. [Pg.551]

Treatment of 2,4,6-tri-rerr-butylphenol with bromine in cold acetic acid gives the compound Ci)jH29BrO in quantitative yield. The infrared spectrum of this compound contains absorptions at 1630 and 1655 cm . Its H NMR spectrum shows only three peaks (all singlets), at 8 1.2, 1.3, and 6.9, in the ratio 9 18 2. What is a reasonable structure for the compound ... [Pg.1023]

At the other end of the spectrum are the ab initio ( from first principles ) methods, such as the calculations already discussed for H2 in Chapter 4. I am not trying to imply that these calculations are correct in any strict sense, although we would hope that the results would bear some relation to reality. An ab initio HF calculation of the potential energy curve for a diatomic Aj will generally give incorrect dissociation products, and so cannot possibly be right in the absolute sense. The phrase ab initio simply means that we have started with a certain Hamiltonian and a set of basis functions, and then done all the intermediate calculations with full rigour and no appeal to experiment. [Pg.173]

Figure 2. Partial 100 MHz P.M.R. Spectrum of 3,4,6-tri-O-acetyl-v-glucal (1) measured for a chloroform -d solution (A normal spectrum of the Hi and H2 resonances respectively (B) frequency sweep spin-decoupled spectrum of the Hi and H2 resonances, with a strong decoupling field centred on the Hs resonance (C), as in (B) above, but with an additional weak radiofrequency field centred on the high field transition of the H2 resonance (D), as in (B) above, but with a weak radiofreauency field centred on the low field transition... Figure 2. Partial 100 MHz P.M.R. Spectrum of 3,4,6-tri-O-acetyl-v-glucal (1) measured for a chloroform -d solution (A normal spectrum of the Hi and H2 resonances respectively (B) frequency sweep spin-decoupled spectrum of the Hi and H2 resonances, with a strong decoupling field centred on the Hs resonance (C), as in (B) above, but with an additional weak radiofrequency field centred on the high field transition of the H2 resonance (D), as in (B) above, but with a weak radiofreauency field centred on the low field transition...
In addition to the above mentioned 4J couplings, we have now observed several examples of couplings across five bonds—i.e. 5J. For example, the ribopyranose derivative (13) shows a coupling of ca. 0.1 Hz between Hx and H4. Further examples occur in the spectrum of 2,3,4-tri-0-acetyl-l,6-anhydro-/ -D-glucopyranose (12), where Ji,4 = ca. 0.1 Hz and J2,5 = 0.5 Hz. Whether it is significant that these couplings all occur between equatorially oriented protons must await further studies. [Pg.253]

The relationship between 20 and reserpine (1) is close like reserpine, intermediate 20 possesses the linear chain of all five rings and all six stereocenters. With the exception of the 3,4,5-tri-methoxybenzoate grouping, 20 differs from reserpine (1) in one very important respect the orientation of the ring C methine hydrogen at C-3 in 20 with respect to the molecular plane is opposite to that found in reserpine. Intermediate 20 is a reserpate stereoisomer, epimeric at position 3, and its identity was secured by comparison of its infrared spectrum with that of a sample of (-)-methyl-O-acetyl-isoreserpate, a derivative of reserpine itself.9 Intermediate 20 is produced by the addition of hydride to the more accessible convex face of 19, and it rests comfortably in a conformation that allows all of the large groups attached to the D/E ring skeleton to be equatorially disposed. [Pg.61]

Luminescence reaction (Viviani et al., 2002a) The luciferin-luciferase luminescence reaction was carried out in 0.1 M Tris-HCl, pH 8.0, containing 2mM ATP and 4mM Mg2+. Mixing luciferase with luciferin and ATP resulted in an emission of light with rapid onset and a kinetically complex decay. Further additions of fresh luciferase, after the luminescence has decayed to about 10% of its maximum value, resulted in additional luminescence responses similar to the initial one (Fig. 1.15). According to the authors, the repetitive light emission occurred in consequence of the inhibition of luciferase by a reaction product, as seen in the case of the firefly system (McElroy et al., 1953). The luminescence spectrum showed a peak at 487nm (Fig. 1.16). [Pg.27]

Fig. 3.1.4 Bioluminescence spectrum of Cypridina luciferin catalyzed by Cypridina luciferase (A), the fluorescence excitation spectrum of oxyluciferin in the presence of luciferase (B), the fluorescence emission spectrum of the same solution as B (C), and the absorption spectrum of oxyluciferin (D). The fluorescence of oxyluciferin alone and luciferase alone are negligibly weak. Measurement conditions A, luciferin (lpg/ml) plus a trace amount of luciferase in 20 mM sodium phosphate buffer, pH 7.2, containing 0.2 M NaCl B and C, oxyluciferin (20 pM) plus luciferase (0.2mg/ml) in 20 mM sodium phosphate buffer, pH 7.2, containing 0.2 M NaCl D, oxyluciferin (41 pM) in 20 mM Tris-HCl buffer, pH 7.6, containing 0.2 M NaCl. All are at 20°C. Fig. 3.1.4 Bioluminescence spectrum of Cypridina luciferin catalyzed by Cypridina luciferase (A), the fluorescence excitation spectrum of oxyluciferin in the presence of luciferase (B), the fluorescence emission spectrum of the same solution as B (C), and the absorption spectrum of oxyluciferin (D). The fluorescence of oxyluciferin alone and luciferase alone are negligibly weak. Measurement conditions A, luciferin (lpg/ml) plus a trace amount of luciferase in 20 mM sodium phosphate buffer, pH 7.2, containing 0.2 M NaCl B and C, oxyluciferin (20 pM) plus luciferase (0.2mg/ml) in 20 mM sodium phosphate buffer, pH 7.2, containing 0.2 M NaCl D, oxyluciferin (41 pM) in 20 mM Tris-HCl buffer, pH 7.6, containing 0.2 M NaCl. All are at 20°C.
Fig. 3.2.4 Fluorescence spectra of F (solid lines), and the bioluminescence spectrum of F plus P, in 20 mM Tris-HCl, pH 7.6, containing 0.15 M NaCl, at 4°C. Both F and P were obtained from Meganyctiphanes norvegica. From Shimomura and Johnson, 1968a. Fig. 3.2.4 Fluorescence spectra of F (solid lines), and the bioluminescence spectrum of F plus P, in 20 mM Tris-HCl, pH 7.6, containing 0.15 M NaCl, at 4°C. Both F and P were obtained from Meganyctiphanes norvegica. From Shimomura and Johnson, 1968a.
Fig. 3.3.1 Luminescence spectrum of coelenterazine catalyzed by the luciferase of the decapod Oplophorus in 15 mM Tris-HCl, pH 8.3, containing 50 mM NaCl (solid line). For comparison, the luminescence catalyzed by the luciferase of the anthozoan sea pansy Renilla is shown with dashed line (in 25 mM Tris-HCl, pH 7.5, containing 0.1 M NaCl). Fig. 3.3.1 Luminescence spectrum of coelenterazine catalyzed by the luciferase of the decapod Oplophorus in 15 mM Tris-HCl, pH 8.3, containing 50 mM NaCl (solid line). For comparison, the luminescence catalyzed by the luciferase of the anthozoan sea pansy Renilla is shown with dashed line (in 25 mM Tris-HCl, pH 7.5, containing 0.1 M NaCl).
Fig. 6.2.4 Change in the absorption spectrum of pholasin (14.5 p,M) caused by the luminescence reaction catalyzed by Pholas luciferase (1.1 p.M). The curve shown is the differential spectrum between a cell containing the mixture of pholasin and Pholas luciferase (0.9 ml in the sample light path) and two cells containing separate solutions of pholasin and the luciferase at the same concentrations (in the reference light path), all in 0.1 M Tris-HCl buffer, pH 8.5, containing 0.5 M NaCl. Four additions of ascorbate (3 iM) were made to the sample mixture to accelerate the reaction. The spectrum was recorded after 120 min with a correction for the base line. From Henry and Monny, 1977, with permission from the American Chemical Society. Fig. 6.2.4 Change in the absorption spectrum of pholasin (14.5 p,M) caused by the luminescence reaction catalyzed by Pholas luciferase (1.1 p.M). The curve shown is the differential spectrum between a cell containing the mixture of pholasin and Pholas luciferase (0.9 ml in the sample light path) and two cells containing separate solutions of pholasin and the luciferase at the same concentrations (in the reference light path), all in 0.1 M Tris-HCl buffer, pH 8.5, containing 0.5 M NaCl. Four additions of ascorbate (3 iM) were made to the sample mixture to accelerate the reaction. The spectrum was recorded after 120 min with a correction for the base line. From Henry and Monny, 1977, with permission from the American Chemical Society.
Fig. 6.3.4 Luminescence spectrum of the Watasenia bioluminescence reaction measured with a crude extract of light organs that contain particulate matters, in chilled 0.1 M Tris-HCl buffer, pH 8.26, containing 1.5 mM ATP. From Tsuji, 2002, with permission from Elsevier. Fig. 6.3.4 Luminescence spectrum of the Watasenia bioluminescence reaction measured with a crude extract of light organs that contain particulate matters, in chilled 0.1 M Tris-HCl buffer, pH 8.26, containing 1.5 mM ATP. From Tsuji, 2002, with permission from Elsevier.
Fig. 6.3.7 Luminescence spectrum of a homogenate of the luminous organ of Symplectoteuthis oualaniensis in the presence of 0.5 M KC1 (from Tsuji and Leisman, 1981). A homogenate suspension (1 ml) and 1MKC1 (1 ml), both made with 50 mM Tris-HCl, pH 7.6, containing 1 mM dithioerythritol, were mixed and the spectrum was measured 6 min after mixing. Note that the luminescence of the photoprotein symplectin isolated from the luminous organs showed a maximum at 470—480 nm (Takahashi and Isobe, 1993, 1994). Fig. 6.3.7 Luminescence spectrum of a homogenate of the luminous organ of Symplectoteuthis oualaniensis in the presence of 0.5 M KC1 (from Tsuji and Leisman, 1981). A homogenate suspension (1 ml) and 1MKC1 (1 ml), both made with 50 mM Tris-HCl, pH 7.6, containing 1 mM dithioerythritol, were mixed and the spectrum was measured 6 min after mixing. Note that the luminescence of the photoprotein symplectin isolated from the luminous organs showed a maximum at 470—480 nm (Takahashi and Isobe, 1993, 1994).
Fig. 7.1.5 Fluorescence spectra of purified Chaetopterus photoprotein (CPA) in 10 mM ammonium acetate, pH 6.7 (solid lines), and the bioluminescence spectrum of the luminous slime of Chaetopterus in 10 mM Tris-HCl, pH 7.2 (dashed line). Note that the luminescence spectrum of Chaetopterus photoprotein in 2 ml of 10 mM Tris-HCl, pH 7.2, containing 0.5 M NaCl, 5 pi of old dioxane and 2 pi of 10 mM FeSC>4 (Amax 453-455 nm) matched exactly with the fluorescence emission spectrum of the photoprotein. No significant change was observed in the fluorescence spectrum after the luminescence reaction. Fig. 7.1.5 Fluorescence spectra of purified Chaetopterus photoprotein (CPA) in 10 mM ammonium acetate, pH 6.7 (solid lines), and the bioluminescence spectrum of the luminous slime of Chaetopterus in 10 mM Tris-HCl, pH 7.2 (dashed line). Note that the luminescence spectrum of Chaetopterus photoprotein in 2 ml of 10 mM Tris-HCl, pH 7.2, containing 0.5 M NaCl, 5 pi of old dioxane and 2 pi of 10 mM FeSC>4 (Amax 453-455 nm) matched exactly with the fluorescence emission spectrum of the photoprotein. No significant change was observed in the fluorescence spectrum after the luminescence reaction.
Fig. 9.9 Luminescence spectrum of a young fruiting body of Fanellus stipticus (1) the chemiluminescence spectra of PM-1 in the presence of CTAB (2) hexadecanoyl-choline iodide (3) and tetradecanoylcholine chloride (4). Chemiluminescence was elicited with Fe2+ and H2O2 in 50mM Tris buffer, pH 8.0, containing 0.18mM EDTA. Fig. 9.9 Luminescence spectrum of a young fruiting body of Fanellus stipticus (1) the chemiluminescence spectra of PM-1 in the presence of CTAB (2) hexadecanoyl-choline iodide (3) and tetradecanoylcholine chloride (4). Chemiluminescence was elicited with Fe2+ and H2O2 in 50mM Tris buffer, pH 8.0, containing 0.18mM EDTA.
Artifact removal and/or linearization. A common form of artifact removal is baseline correction of a spectrum or chromatogram. Common linearizations are the conversion of spectral transmittance into spectral absorbance and the multiplicative scatter correction for diffuse reflectance spectra. We must be very careful when attempting to remove artifacts. If we do not remove them correctly, we can actually introduce other artifacts that are worse than the ones we are trying to remove. But, for every artifact that we can correctly remove from the data, we make available additional degrees-of-freedom that the model can use to fit the relationship between the concentrations and the absorbances. This translates into greater precision and robustness of the calibration. Thus, if we can do it properly, it is always better to remove an artifact than to rely on the calibration to fit it. Similar reasoning applies to data linearization. [Pg.99]

In a similar system, the reaction of the ferric(edta) complex with peroxycarboxylic acids was probed by adding 2,4,6-tri-fe/r-butyl phenol, ArOH.2 This experiment gave rise to the aryloxyl radical, ArO, which persisted for hours and was detected by its characteristic spectrum. It was indeed formed in the reaction mentioned, at a rate that was independent of [ArOH], It was proposed that ArO results from a reactive oxo-iron intermediate, tentatively (edta)FevO. [Pg.102]

A 100 MHz. proton magnetic resonance spectrum (chloroform d) of the amine in the presence of an equal amount of the chiral shift reagent, tris[3-(trifluoromethylhydroxymethylene)-d-camphorato]euro-pium(III)4 (submitters), or in the presence of an equal amount of tris[3-(heptafluoropropylhydroxymethylene)-d-camphorato]europium-(III) (checkers), revealed that the product contained no detectable enantiomeric isomer. [Pg.82]


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See also in sourсe #XX -- [ Pg.228 , Pg.229 , Pg.230 , Pg.231 , Pg.232 , Pg.233 , Pg.234 , Pg.235 , Pg.236 , Pg.237 , Pg.238 ]




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Luminescence spectra tris

Spectra of tris

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