Latest research results: new technology to crack protein

Researchers from the US Department of Energy's (DOE) Lawrence Berkeley National Laboratory (Berkeley Lab) have published a leaping achievement that will enable scientists to better understand the structural state of large molecules such as proteins in solution.

The researchers used X-ray (SAXS) or neutron (SANS) SAS small-angle scattering experimental data to develop a new set of indicators that will reduce the time required by up to 20 times. According to the author Robert Rambo, "SAS is the only technology that can reflect the complete thermodynamic state of large molecules in a single image." "In previous studies, SAS analysis focused mainly on particles in discrete structural states", "However, for biology, many proteins and protein complexes are not obediently obedient, they may be very variable, resulting in diffuse Type of structural state. Our new set of metrics applies to all particle types. "

The research results were published in the journal Nature. Another author of the article, John A. Tainer said, "In this paper in Nature, the SAS indicators that we report will analyze the variable molecular machinery that regulates cell biology, as well as the precise high-throughput analysis. Large impact. "SAS imaging uses X-rays or neutrons to penetrate the sample to create small collisions between the X-rays or neutrons and the sample ’s nano- or sub-nanometer-sized particles, and then detects how these collisions scatter to determine the particles. Shape and size. This method is easier to apply to macromolecular complexes than X-ray crystallography, and is particularly useful for proteins and complexes with high flexibility. In this article, the analysis standard created by Rambo and Tainer is formulated by a constant SAS, which means that its value will not change with the measurement method and measurement location, this invariant is called "volume correlation "Volume-of-correlation", its value is the intensity of scattering from X-rays or Chinese characters, corresponding to the structural state of the particles, and it has nothing to do with its concentration and complex. This correlation is used for proteins that have changed shape, and these data sets are used to help traditional SAS analysis results be more reliable, thereby confirming the accuracy of this structure obtained from the solution. This optimization enhances the internal capabilities of SAS for high-throughput analysis, and should expand its application to flexible macromolecules and nanoparticles in research solutions. Rombo said, "According to this measurement standard, it may be possible to collect and analyze SAS data from the theoretical limit." This means that we can reduce the time for data collection, and the 90-minute time required by the instrument can be reduced to 9 minutes.

Tainer also added, "This discovery is the first result of X-ray scattering invariants, and the new discovery of volume-dependent invariants also opens a window for future analysis of variable biological samples."

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