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This experiment is a classic chemistry demonstration that can be used in laboratory courses as a general chemistry experiment to study chemical kinetics and reaction mechanism. [2] The reaction also works with other reducing agents besides glucose [3] and other redox indicator dyes besides methylene blue. [4]
The result of a DSC experiment is a curve of heat flux versus temperature or versus time. There are two different conventions: exothermic reactions in the sample shown with a positive or negative peak, depending on the kind of technology used in the experiment. This curve can be used to calculate enthalpies of transitions. This is done by ...
Pulse-chase analysis of auxin signal transduction in an Arabidopsis thaliana wildtype and an axr2-1 mutant. Wild-type and axr2-1 seedlings were labeled with 35S-methionine, and AXR2/axr2-1 protein was immunoprecipitated either immediately after the labeling period (t = 0) or following a 15-minute chase with unlabeled methionine (t = 15).
A replica of an apparatus used by Geiger and Marsden to measure alpha particle scattering in a 1913 experiment. The Rutherford scattering experiments were a landmark series of experiments by which scientists learned that every atom has a nucleus where all of its positive charge and most of its mass is concentrated.
The next stage of muon g − 2 research was conducted at the Brookhaven National Laboratory (BNL) Alternating Gradient Synchrotron; the experiment was known as (BNL) Muon E821 experiment, [17] but it has also been called "muon experiment at BNL" or "(muon) g − 2 at BNL" etc. [7] Brookhaven's Muon g − 2 experiment was constructed from 1989 to 1996 and collected data from 1997 to 2001.
[A 2] Of this experiment, Albert Einstein wrote, "If the Michelson–Morley experiment had not brought us into serious embarrassment, no one would have regarded the relativity theory as a (halfway) redemption." [A 3]: 219 Michelson–Morley type experiments have been repeated many times with steadily increasing sensitivity.
Proteins of the erythrocyte membrane separated by SDS-PAGE according to their molecular masses. SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.
Below is a table of amino acids produced and identified in the "classic" 1952 experiment, as analyzed by Miller in 1952 [3] and more recently by Bada and collaborators with modern mass spectrometry, [7] the 2008 re-analysis of vials from the volcanic spark discharge experiment, [7] [55] and the 2010 re-analysis of vials from the H 2 S-rich ...