Can you use spectrophotometry to determine the concentration of the nucleoprotein?
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If you have a purified prep of chromatin, you can use the spec to measure the amount of protein at 254 nm.  The problem is that this overlaps with DNA absorbance (260/280nm).  You can use a protein assay such as bradford or BCA to measure protein concentration.  Usually western blots are used to measure relative protein concetrations of specific proteins ie histone, actin.
560605
With IR you can dilute your soln so you have a bit more of it and then stick it on a plate and check out the peaks. That can give you a good idea of what you have... or there is HNMR, and CNMR, but it really depends on how much you have of the substance. If you have a general idea of what it might be then check the PH and give it a good guess... or use an indicator that might form some kind of ppt. with the substance in the soln . I've found that a refractive index really isnt the way to go because it isnt as reliable as other tests. Gas chromotograpy and Thin layer chormotograpy both require a general idea of what you might be coming up with... GC can be sketchy and you dont want to loose any sample on a test that might not tell you much, same with TLC, you would haev to be careful with the slovent interaction with the "unknown" that you have.
190406
most likely unless u want to be precise the the nanogram\nthen i could go either way depending on how much atoms are in them
402176
You're right, spectroscopy is the proper method...Below you'll find a link to a quick and simple explanation.
207923
I believe you run a blank sample and assume the resulting spectograph as 0  then using the spectrograph of your unknown using the Peaks  calculate the response factors then concentration.
849528
In order to perform in vitro analyses, a protein must be purified away from other cellular components. This process usually begins with cell lysis, in which a cell's membrane is disrupted and its internal contents released into a solution known as a crude lysate. The resulting mixture can be purified using ultracentrifugation, which fractionates the various cellular components into fractions containing soluble proteins; membrane lipids and proteins; cellular organelles, and nucleic acids. Precipitation by a method known as salting out can concentrate the proteins from this lysate. Various types of chromatography are then used to isolate the protein or proteins of interest based on properties such as molecular weight, net charge and binding affinity. The level of purification can be monitored using gel electrophoresis if the desired protein's molecular weight is known, by spectroscopy if the protein has distinguishable spectroscopic features, or by enzyme assays if the protein has enzymatic activity.\n\nFor natural proteins, a series of purification steps may be necessary to obtain protein sufficiently pure for laboratory applications. To simplify this process, genetic engineering is often used to add chemical features to proteins that make them easier to purify without affecting their structure or activity. Here, a "tag" consisting of a specific amino acid sequence, often a series of histidine residues (a "His-tag"), is attached to one terminus of the protein. As a result, when the lysate is passed over a chromatography column containing nickel, the histidine residues ligate the nickel and attach to the column while the untagged components of the lysate pass unimpeded.\n\n\n[edit] Cellular localization\n \nProteins in different cellular compartments and structures tagged with green fluorescent protein.The study of proteins in vivo is often concerned with the synthesis and localization of the protein within the cell. Although many intracellular proteins are synthesized in the cytoplasm and membrane-bound or secreted proteins in the endoplasmic reticulum, the specifics of how proteins are targeted to specific organelles or cellular structures is often unclear. A useful technique for assessing cellular localization uses genetic engineering to express in a cell a fusion protein or chimera consisting of the natural protein of interest linked to a "reporter" such as green fluorescent protein (GFP). The fused protein's position within the cell can be cleanly and efficiently visualized using microscopy, as shown in the figure opposite.\n\nThrough another genetic engineering application known as site-directed mutagenesis, researchers can alter the protein sequence and hence its structure, cellular localization, and susceptibility to regulation, which can be followed in vivo by GFP tagging or in vitro by enzyme kinetics and binding studies.\n\n\n[edit] Proteomics and bioinformatics\nMain articles: Proteomics and Bioinformatics\nThe total complement of proteins present in a cell or cell type is known as its proteome, and the study of such large-scale data sets defines the field of proteomics, named by analogy to the related field of genomics. Key experimental techniques in proteomics include protein microarrays, which allow the detection of the relative levels of a large number of proteins present in a cell, and two-hybrid screening, which allows the systematic exploration of protein-protein interactions. The total complement of biologically possible such interactions is known as the interactome. A systematic attempt to determine the structures of proteins representing every possible fold is known as structural genomics.\n\nThe large amount of genomic and proteomic data available for a variety of organisms, including the human genome, allows researchers to efficiently identify homologous proteins in distantly related organisms by sequence alignment. Sequence profiling tools can perform more speci
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Yes. It produces a bright yellow precipate:\nAgNO3 (aq) + KI (aq) → KNO3 (aq) + AgI (ppt)
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I don't know how you are precipitating out the gold, but I don't think a colorimetric test for gold in solution is possible.  It is non-reactive and does not ionize.  Given that gold has filled upper electron orbitals, you might be able to run a UV-VIS spectrum and get some UV absorption for solvated gold versus clean aqua regia.  The UV apsorption is probably going to be in the lower UV wavlengths, and it might not be possible to differentiate between trace levels of gold and trace levels of transition metal impurities.\n\nIf you are precipitating the gold by an equilibrium process, just load up on your precipitation compound to push the equilibrium as far as possible to one side.  Another possibility is to electrolytically remove any trace gold from the aqua regia.  Sorry I don't have any better suggestions.
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For some values of difficult to test.\n\nTypically, inorganic compounds are ionic in nature, so you're more likely to get chlori*d*e than chlorine (you do appreciate the difference, right?) so you can do things like addition of silver nitrate to get a ppt.\n\nHowever, you can also run mass specs and things - chlorine has a typical splitting pattern here based on isotopic ratios and so in this instance it's probably just as easy to detect it in organic (if not more so) than in inorganic compounds
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In theory a DNA sample could be used to predict hair and eye color with reasonable accuracy, although we do not currently have a data base matching these phenotypes with allelic sequences.  However, when it comes to more complex morphological features (height, weight, shape of facial features, etc.), it would be virtually impossible to predict as the effects of environmental factors are enormous.\n\nWe do not currently have the ability to predict the conformation of a protein that would result from a particular sequence, and thus cannot determine the function except through direct experimental means or comparison with an identical sequence whose function has been experimentally determined.
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In physics,spectrophotometry is the quantitative study of electromagnetic spectra. It is more specific than the general term electromagnetic spectroscopy in that spectrophotometry deals with visible light, near-ultraviolet, and near-infrared. Also, the term does not cover time-resolved spectroscopic techniques.\nSpectrophotometry involves the use of a spectrophotometer. A spectrophotometer is a photometer (a device for measuring light intensity) that can measure intensity as a function of the color, or more specifically, the wavelength of light. There are many kinds of spectrophotometers. Among the most important distinctions used to classify them are the wavelengths they work with, the measurement techniques they use, how they acquire a spectrum, and the sources of intensity variation they are designed to measure. Other important features of spectrophotometers include the spectral bandwidth and linear range.\n\nPerhaps the most common application of spectrophotometers is the measurement of light absorption, but they can be designed to measure diffuse or specular reflectance. Strictly, even the emission half of a luminescence instrument is a kind of spectrophotometer.\n\nThere are two major classes of spectrophotometers; single beam and double beam. A double beam spectrophotometer measures the ratio of the light intensity on two different light paths, and a single beam spectrophotometer measures the absolute light intensity. Although ratio measurements are easier, and generally stabler, single beam instruments have advantages; for instance, they can have a larger dynamic range.\n\nVisible-region spectrophotometers\n\nVisible region 400-700nm spectrophotometry is used extensively in colorimetry science. Ink manufacturers, printing companies, textiles vendors, and many more, need the data provided through colorimetry. They usually take readings every 10 nanometers along the visible region, and produce a spectral reflectance curve. These curves can be used to test a new batch of colorant to check if it makes a match to specifications. Traditional visual region spectrophotometers cannot detect if a colorant has fluorescence. This can make it impossible to manage color issues if one or more of the printing inks is fluorescent. Where a colorant contains fluorescence, a bi-spectral fluorescent spectrophotometer is used. There are two major setups for visual spectrum spectrophotometers, d/8 (spherical) and 0/45. The names are due to the geometry of the light source, observer and interior of the measurement chamber. Scientists use this machine to measure the amount of compounds in a sample. If the compound is more concentrated more light will be absorbed by the sample.\n\ncomponents: 1. The light source shines through the sample. 2. The sample absorbs light. 3. The detector detects how much light the sample has absorbed. 4. The detector then converts how much light the sample absorbed into a number.\n\n[edit] Spectroradiometers\nSpectrographic representation of the light output of an incandescent bulb (left) and a fluorescent lamp (right)\nSpectrographic representation of the light output of an incandescent bulb (left) and a fluorescent lamp (right)\n\nSpectroradiometers, which operate almost like the visible region spectrophotometers, are designed to measure the spectral density of illuminants in order to evaluate and categorize lighting for sales by the manufacturer, or for the customers to confirm the lamp they decided to purchase is within their specifications.\n[edit] UV and IR spectrophotometers\n\nThe most common spectrophotometers are used in the UV and visible regions of the spectrum, and some of these instruments also operate into the near-infrared region as well. Spectrophotometers designed for the main infrared region are quite different because of the technical requirements of measurement in that region. One major factor is the type of photosensors that are available for different spectral regions, but infrared measurement
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Ummm...You will have to figure out which is faster... but I can give an idea as to proceedure...First, try to answer this question: What are all the colored species in grape juice? You need to know that first. Hopefully there is only one. That would simplfy things. Then you need an extinction coefficient for that compound, if you can find one. Using that, you can take several absorbance measures and use Beer's law to establish the concentration of that species in your stock solution. Beer's law states that Absorbance = extinction coefficient x concentration x path length. Your path length is the width of your cuvette, which is usually 1 cm. Beer's Law will not be valid if you use a solution that is so concentrated that it gives you an absorbance value greater than 2. At Absorbance = 2, well over 99% of light is being absorbed. A reading over 2 is thus considered analytically unusable. Your juice can be diluted, if necessary, with DEIONIZED (aka distilled) water. Once you do that, I would roughly time each reaction by just looking at it with my eye, adding just a drop or so of bleach/peroxide initially, and increasing the amount only if necessary. Make sure to add exactly the same amount of bleach/peroxide to exactly the same volume of grape juice. Once you have the reaction basically set up to your satisfaction, then place your juice sample in the colorimeter and get ready to add your reagent. Remember to take a measurement before you add any bleach/peroxide for EACH of the two tests. And take your measurements on the same time frame (ex: every 30 sec.)Good Luck!!! :-)
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By serum protein electrophoresis, or by subtracting Serum albumin value from serum total protein value
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thats not so hard... all you have to do is titrate it against an acidic solution of known concentration that has a mole ratio of 1:1with sls. add a indicator ( phenolphthaleine) to find the endpoint and that should do it.
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You could use a turbidometric method that could detect the diffraction of light through the liquid and correlate it with the amount of microbial growth in it.  \n\nYou could also use a calibrated loop to plate the liquid and then count colonies.  I know they do this with urine cultures in hospital labs at times.  The loop picks up a certain amount of liquid like 10 microliters or so and then you can correlate the growth with this 10 microliter figure.
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(1) Take a container and measure the length of the container. Let us say the length of the container is L. \n\n(2) Take a beam of light (preferably a monochromatic source like laser beam) and shine it through the empty container. \n\n(3) Measure the intensity of the light at the end where the beam has gone through the empty container. Let this be Io. \n\n(4) Now fill the container with the liquid whose molar extinction coefficient is unknown. Now measure the light intensity as the beam travels the length L of the container. The measured intensity is I.\n\n(5) Beer-Lamberts law is I=Io exp(-a L) where all the quantities have been experimentally determined except a which is the extinction coefficient. \nRearrange the above formula and we get, a=(-1/L)*log(I/Io) where log is to the base e.
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use spectrophotometric method(uv-vis spectrometry).Few things u shud remember.....\n1) Use Labert-Beer's law\n2) u shud know the molar extingtion coefficient value of that particular species\n3) concentration of the species\n4) Calculate lambdamax. using LB law\nIt is an indirect method.\n\nUV-VIS. Spectroscopy will give u the lambdamax value directly...alongwith absorbance