terpenoids structure determination by spectroscopy?
404848
2D 1H-13C NMR and a high-res mass spec are all you need.
220155
Are you asking for an explnation for the spectral proprties  or doy ou want the actual spectral report? either way go here....http://orgchem.colorado.edu/hndbksupport/irtutor/estersir.html
1096886
www.thespectrum.net\n\nhope this helped
590885
sorry friend, but this not a question with a simple answer. yes, i know somebody who can interpret nmr spectra, but it involves a lot of computation. there are even whole journals devoted to it, so if it is urgent, you have lost.
232394
Looking at the name, its probably a ketone.  Ketones usually have a double bond which makes the compond have a "Y" shape.  The stem of the Y is where the double bond is.
424471
Triterpenes consist of six isoprene units and have the molecular formula C30H48. The linear triterpene squalene, the major constituent of shark liver oil, is derived from the reductive coupling of two molecules of farnesyl pyrophosphate. Squalene is then processed biosynthetically to generate lanosterol, the structural precursor to all the steroids.Terpenes are derived biosynthetically from units of isoprene, which has the molecular formula C5H8. The basic molecular formulas of terpenes are multiples of it, (C5H8)n where n is the number of linked isoprene units. This is called the isoprene rule or the C5 rule. The isoprene units may be linked together "head to tail" to form linear chains or they may can be arranged to form rings. One can consider the isoprene unit as one of nature's preferred building blocks.\n\nIsoprene itself does not undergo the building process, but rather activated forms, isopentenyl pyrophosphate (IPP or also isopentenyl diphosphate) and dimethylallyl pyrophosphate (DMAPP or also dimethylallyl diphosphate), are the components in the biosynthetic pathway. IPP is formed from acetyl-CoA via the intermediacy of mevalonic acid in the HMG-CoA reductase pathway. IPP can then be isomerized to DMAPP by the enzyme isopentenyl pyrophosphate isomerase.\n*PAL,Phenylalanine ammonia-lyase from parsley is post translationally modified by dehydrating its Ser-202 to the catalytically essential dehydroalanine prosthetic group. The codon of Ser-202 was changed to those of alanine and threonine by site-directed mutagenesis. These mutants and the recombinant wild-type enzyme, after treatment with sodium borohydride, were virtually inactive with L-phenylalanine as substrate but catalyzed the deamination of L-4-nitrophenylalanine, which is also a substrate for the wild-type enzyme. Although the mutants reacted about 20 times slower with L-4-nitrophenylalanine than the wild-type enzyme, their Vmax for L-4-nitrophenylalanine was two orders of magnitude higher than for L-phenylalanine. In contrast to L-tyrosine, which was a poor substrate, DL-3-hydroxyphenylalanine (DL-m-tyrosine) was converted by phenylalanine ammonia-lyase at a rate comparable to that of L-phenylalanine. These results suggest a mechanism in which the crucial step is an electrophilic attack of the prosthetic group at position 2 or 6 of the phenyl group. In the resulting carbenium ion, the ß-HSi atom is activated in a similar way as it is in the nitro analogue. Subsequent elimination of ammonia, concomitant with restoration of both the aromatic ring and the prosthetic group, completes the catalytic cycle.
890060
This solution probably has fluorescence at UV (ultra violet) wave length. try looking at it in a room with red light, if there is no light using the lenses then it's confirmed. but you can't simply identify it this way. you have to know the exact wave length that it has fluorescence at. even then you might not be able to identify it. try using UV-visible spectroscopy and when you have its spectra, you can identify it. for more information see: principles of instrumental analysis by Skoog
800470
That depends on your research study. Use NMR to obtain physical, chemical, electronic and structural information about a molecule. This is the only technique that can provide detailed information on the exact three-dimensional structure of biological molecules in solution. \n\nMass spectrometry on the other hand,  is used to measure the mass-to-charge ratio of ions. It is most generally used to find the composition of a physical sample by generating a mass spectrum representing the masses of sample components. It can also be used in these applications:\n\n-identifying unknown compounds by the mass of the compound molecules or their fragments \n-determining the isotopic composition of elements in a compound \n-determining the structure of a compound by observing its fragmentation \n-quantifying the amount of a compound in a sample using carefully designed methods (mass spectrometry is not inherently quantitative) \n-studying the fundamentals of gas phase ion chemistry (the chemistry of ions and neutrals in vacuum) \n-determining other physical, chemical or even biological properties of compounds with a variety of other approaches
178785
Disregard the previous gibberish.\nTo estimate purity you need to be able to interpret the spectrum to determine which peaks belong to your product.  Assuming that you can do this, the entire spectrum needs to be integrated and from the integrals of the individual peaks you can determine the ratio of impurities present and thereby estimate the purity of your product.
353617
Optical Spectrum Analyzer (OSA) is probably what you're looking for...nice for discovering chemical composition of light source and probably a zillion other different things.
681864
alkyl phenyl ketone in trivial nomenclature, and phenyl alkanone in iupac
376071
This site should help\n\nhttp://ww2010.atmos.uiuc.edu/(Gh)/guides/mtr/cld/cldtyp/home.rxml
183009
Get the CAS number.  Look it up on Chemfinder.
492448
G E R A N Y L GERANIOL has been proposed by some\nauthors as an intermediate in the biosynthesis of di- and\ntricyclic diterpenes.\n\nAccording to Wagner and Jaureg  and Kuhn and\nGrundmann  it would be transformed into phytol by\nhydrogenation and into lycopene and other carotenoids\nby dehydration and dimerization. Ruzicka suggested \nthat geranyl geraniol and geranyl linalool might be the\nprecursors of the di- and tricyclic diterpenes respectively ;\nbut although geranyl linalool has been isolated, together\nwith phytol and isophytol, from jasmine essential oil by\nDemole and Lederer , these authors were unable to\nisolate geranyl geraniol from the same source, probably\nbecause it is rapidly metabolized.\nAccording to some recent work of Costes , geranyl\ngeraniol and geranyl linalool are precursors of carotene\nand lutein. Stobbe  has proposed geranyl geraniol as\nan intermediate in the biosynthesis of vitamin Kz.\nPopjak  has found, by gas-liquid chromatography\nof the unsaponifiable fraction of liver homogenate incubated\nwith ~~-mevalonate-2-"C, two peaks with the\nretention volumes expected for geranyl linalool and\ngeranyl geraniol. These were minor constituents of a\nmixture consisting predominantly of nerolidol, alltrans\nfarnesol, methyl allyl alcohol, linalool, nerol, and\ngeraniol.\nGeranyl geraniol has, to our knowledge, never been\nisolated from natural sources and fully characterized although\nit has been shown to be synthesized by cell-free\nenzyme systems . This article describes the isolation\nand identification of geranyl geraniol from the unsaponifiable\nfraction of linseed oil. We have also obtained\nit from the corresponding fraction of peanut oil.\n\nFor the separation of the unsaponifiable fraction, an\nItalian linseed oil was utilized. For comparison, samples\nof phytol and farnesol were purchased from British Drug\nHouses (Poole, England) and Fluka A.G. (Basel,\nSwitzerland).\nColumn Chromatography. Alumina (Activity 111) in\npetroleum ether (bp 60-80°C) was used to fractionate\nthe unsaponifiable fraction, and silicic acid (Mallinckrodt\nChemical Company, St. Louis, Mo.) for the separation\nof phytol from geranyl geraniol. Details are given in\nResults. After separation, each fraction was recovered\nand weighed, and its composition was checked by TLC.\nFor thin-layer chromatography, 20 X 20 cm plates, 0.25\nmm thick, prepared with Silica Gel G (Merck & Co.,\nInc.) were used. Substances were detected by charring\nwith sulfuric acid or spraying with 2,7-dichlorofluorescein\n(sodium salt) in alcohol.\nGas liquid chromatography :\nBoth polar and nonpolar\ncolumns were used. The nonpolar coliiinn was used in a\nFractovap model C-AID/F chromatograph (Erba,\nMilan) with flame ionization dctcctor. It was 2 m X 4\nmm I.D. and contained SE-30 (methylpolysiloxy giiin,\nGeneral Electric), 1% on silanized Gas-Chrom P,\n100-200 mesh, at 190°C. The flash heater was at 250'C\nand the carrier gas was nitrogen, 40 ml/inin.\nThe polar coluinn, in a Fractovap model B with\nthermal conductivity detector, contained ethylene glycol\nsuccinate polyester, 20% on Chrornosorb W, 60-80\nmesh. Column, 210'C. Flash hcatcr, 250°C. Carrier gas.\nhelium, 4.5 liters/hr.\nInfrared spectra were recorded on a Perkin-Elmer\nInfracord apparatus.
1134842
a fat molecule triacylglycerol
302188
The amino and carboxyl protons are very difficult to observe. Using 100% D2O will replace the carboxyl and amino protons with 2H, and you won't see anything. Use a different solvent and you can't be sure you are in the zwitterion form (pH is difficult to control in non-aqueous solutions and you will get different hydrogen bonding)\n\nIf you really want to see those protons your best bet would be to use 90% H2O / 10% D2O with either phosphate buffer or the perdeuterated buffer of your choice (you can get these from Cambridge Isotopes). Make sure the buffer concentration is large compared to your amino acid, and make sure you have adjusted the pH to the zwitterion range. When you aquire the spectrum you will need to use a water suppression sequence. Presat is the easiest, although I much prefer gradient selected 3-9-19. This still may not be enough to see the protons-- if they are exchanging the linewidth may become so broad as to disappear into the baseline.\n\nWhile it's difficult to observe the carboxyl and amino protons (they are *very* sensitive to solvent and pH) you should be able to see changes in the chemical shifts of the remaining protons, particularly the alpha protons.\n\nIf you are really interested, make a sample of your favorite amino acid and take spectra over a range of pH. Plot the chemical shifts of the visible protons as a function of pH and the shape of the curve should allow you to determine the pKa of the amino and carboxyl groups. Here you could get away with just using D2O, which makes the spectroscopy much simpler.\n\nGood luck and have some fun with this!
276161
click here to view IR spectra of ortho http://www.aist.go.jp/RIODB/SDBS/cgi-bin/cre_frame_disp.cgi?spectrum_type=ir&sdbsno=2650 and para http://www.aist.go.jp/RIODB/SDBS/cgi-bin/cre_frame_disp.cgi?spectrum_type=ir&sdbsno=2681 isomers of nitrophenol.\nIR spectroscopy is very much dependent on the polarity of a bond and also on the symmetry (and lack of symmetry) of the molecule or a group of atoms in a molecule. IR spectroscopy is very useful for differentiating the two isomers. I hope you find them.