what are sites to visuavalise right circularly polarised light?
958515
You can try the following web sites:\n\nhttp://www.glenbrook.k12.il.us/GBSSCI/PHYS/CLASS/light/u12l1e.html\n\nhttp://www.uwgb.edu/dutchs/petrolgy/genlight.htm
937754
Something involving atomic spectra.  For example see\nhttp://www.fas.harvard.edu/~scdiroff/lds/QuantumRelativity/StreetLampSpectra/StreetLampSpectra.html
660207
I Think www.sailorcosmos.net has galleries of the Sailor Star Lights.
306417
Circular dichroism (CD), is the differential absorption of left- and right-handed circularly polarized light. It is a form of spectroscopy used to determine the optical isomerism and secondary structure of molecules.\n\nAt a given wavelength,\n\nΔA = (AL − AR) \nwhere ΔA is the difference between absorbance of left circularly polarized (LCP) and right circularly polarized (RCP) light (this is what is usually measured). It can also be expressed as:\n\nΔA = (εL − εR) C l \nwhere εL and εR are the molar extinction coefficients for RCP and LCP light, where C is the molar concentration and l is path length.\n\nThen\n\nΔε = (εL − εR) \nis the molar circular dichroism. This is what is usually meant by the circular dichroism of the substance.\n\nAlthough ΔA is usually measured, for historical reasons most measurements are reported in degrees of ellipticity.\n\nThe molar ellipticity is:\n\n[θ] = 3298Δε. \nIn general, this phenomenon will be exhibited in absorption bands of any optically active molecule. As a consequence, circular dichroism is exhibited by biological molecules, because of the dextrorotary (e.g. some sugars) and levorotary (e.g. some amino acids) molecules they contain. Noteworthy as well is that secondary structure will also impart a distinct CD to their respective molecules. Therefore, the alpha helix of proteins and the double helix of nucleic acids have CD spectral signatures representative of their structures.\n\nCD is closely related to the optical rotary dispersion (ORD) technique, and is generally considered to be more advanced. CD is measured in or near the absorption bands of the molecule of interest, while ORD can be measured far from these bands. In principle these two spectral measurements can be interconverted through an integral transform, if all the absorptions are included in the measurements.\n\nThe ultraviolet CD spectrum of proteins can predict important characteristics of their secondary structure. CD spectra can be readily used to estimate the fraction of a molecule that is in the alpha-helix conformation, the beta-sheet conformation, the beta-turn conformation, or some other (random) conformation. These fractional assignments place important constraints on the possible secondary conformations that the protein can be in. CD cannot, in general, say where the alpha helices that are detected are located within the molecule or even completely predict how many there are. Despite this, CD is a valuable tool, especially for showing changes in conformation. It can, for instance, be used to study how the secondary structure of a molecule changes as a function of temperature or of the concentration of denaturing agents. In this way it can reveal important thermodynamic information about the molecule that cannot otherwise be easily obtained. Anyone attempting to study a protein will find CD a valuable tool for verifying that the protein is in its native conformation before undertaking extensive and/or expensive experiments with it. Also, there are a number of other uses for CD spectroscopy in protein chemistry not related to alpha-helix fraction estimation. s\n\nCD spectroscopy is usually used to study proteins in solution, and thus it complements methods that study the solid state. This is also a limitation, in that many proteins are embedded in membranes in their native state, and solutions containing membrane structures are often strongly scattering. CD is sometimes measured in thin films.\nCD has also been studied in carbohydrates, but with limited success due to the experimental difficulties associated with measurement of CD spectra in the vacuum ultraviolet (VUV) region of the spectrum (100-200 nm), where the corresponding CD bands of unsubstituted carbohydrates lie. Substituted carbohydrates with bands above the VUV region have been successfully measured.\n\nMeasurement of CD is also complicated by the fact that typical aqueous buffer systems often absorb in the range where structur
1144714
This is the way they reflect light.
965176
http://www.glenbrook.k12.il.us/GBSSCI/PHYS/CLASS/light/u12l1e.html
895656
Hi. You could start here : http://www.mellesgriot.com/products/optics/oc_3.htm\nMay not be the best for everyone.
540154
in google, try:\n\neasy LED projects\n\nor\n\nLED firefly art
10757
Use google image search. \nHere's a nice one \nhttp://web.lemoyne.edu/~hevern/psy340/graphics/homunculus.jpg\nbut there are many others. Make sure to ask for permission, or see at the site if they support fair use.
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low glare non-fluorescent true color would be the ideal, I like neodynium bulbs myself.
85548
Polarized  Unpolar.  Magnifying  Difracting Refracting Magnifying
174710
It's a FresnelC function.  Check out the link.
233941
http://pqasb.pqarchiver.com/skyandtelescope/advancedsearch.html
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http://www.industriallasers.net/?source=google&gclid=CMSW1ePGhIQCFRIbIgod9QqTeQ
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Light is refracted from a single point. Since the light which gets refracted into the same colors is all the same distance from the point source, a circle is formed.\n\n-Wied
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Edmunds Scientific\n--> http://scientificsonline.com/search.asp?t=ss&ss=strobe
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try netdetective.  that sight is reliable.