Protein
Nov. 15, 2011
Cobolt has announced the release of the Dual Combiner 473+594 nm which is optimized for high-end Optogenetics research applications.
This version of the Cobolt Dual Combiner offers two emission wavelengths for light-activated proteins: 473nm (up to 50mW) and 594 nm (up to 100mW) from one small box.
moreJun. 10, 2011
JPK Instruments has reported on the work from the Pharmaceutical Sciences Department of the Medical School at the University of Nebraska. The Department has selected the JPK ForceRobot 300 system to extend their studies applying atomic force microscopy in the measurement of single molecule force spectroscopy.
moreNov. 01, 2010
Using intense beams of x-rays at the U.S. DOE Brookhaven National Laboratory, researchers have uncovered the atomic structure of a protein responsible for closing the "mouths," or stomata, of plants. These molecular photographs could help scientists understand how plants will respond to environmental changes facing our planet, such as drought and escalating levels of carbon dioxide and ozone. The study, led by researchers at Columbia University and the New York Structural Biology Center, is published in the October 28, 2010, issue of the journal Nature.
moreNov. 04, 2009
Proteins that copy and edit DNA help protect cells from attack by removing viral DNA insertions. They are thought to reach their target sequence by "sliding", "hopping" and "jumping" along DNA strands. Observing this behavior has proved hard, however, due to its speed of action. We discuss a recent research project that used a high-speed camera to observe - for the first time - the sliding and jumping of EcoRV, a restriction enzyme, along DNA molecules.
moreDec. 01, 2008
Protein Functionality Lifetime in Quantitative FCS: In quantitative fluorescence correlation spectroscopy (FCS) in vitro experiments, D. Zhang and colleagues and have detected concentration decreases in fluorescent protein solutions even in sample preparations with adsorption-protected interfaces. This indicates a loss of protein functionality. By adding compounds with surfactant behaviour, the lifetime of functional fluorescent proteins could be increased 1000-fold even though there do not seem to be direct interactions between protein and surfactant.
Biophys. J. 95, 3439-3446
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