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Marker ski bindings from the 1990s to 2000s. In 2007, Marker unveiled a new freeski binding system called the Duke. Complemented by the Jester, the new system redefined the performance parameters for freeride bindings. In 2008, the company released two new bindings, the Baron and the Griffon, that are also based on the Duke system.
Alpine ski bindings have two functions: 1) Retaining the ski boot on the ski, 2) Releasing the ski boot from the ski in case of a fall to prevent injury to the skier. [11] The retention function typically involves stepping into the binding toe-first and pressing down with the heel of the ski boot, which causes a latch to engage the heel.
There are two common methods in which to construct a DNA molecular-weight size marker. [3] One such method employs the technique of partial ligation. [3] DNA ligation is the process by which linear DNA pieces are connected to each other via covalent bonds; more specifically, these bonds are phosphodiester bonds. [4]
A ligand binding assay (LBA) is an assay, or an analytic procedure, which relies on the binding of ligand molecules to receptors, antibodies or other macromolecules. [1] A detection method is used to determine the presence and amount of the ligand-receptor complexes formed, and this is usually determined electrochemically or through a fluorescence detection method. [2]
S. cerevisiae septins revealed with fluorescent microscopy utilizing fluorescent labeling. In molecular biology and biotechnology, a fluorescent tag, also known as a fluorescent label or fluorescent probe, is a molecule that is attached chemically to aid in the detection of a biomolecule such as a protein, antibody, or amino acid.
DIG-binding proteins. Tinberg et al. designed artificial proteins that bind DIG. Their best binder, DIG10.3, was a 141 amino acid protein that bound DIG with a dissociation constant (K d) of 541 (+/- 193) pM. [5] Anti-digoxigenin antibodies with high affinities and specificity are used in a variety of biological immuno-assays (e.g. ELISA). The ...
Maxam–Gilbert sequencing requires radioactive labeling at one 5′ end of the DNA fragment to be sequenced (typically by a kinase reaction using gamma-32 P ATP) and purification of the DNA. Chemical treatment generates breaks at a small proportion of one or two of the four nucleotide bases in each of four reactions (G, A+G, C, C+T).
PECAM-1 is a highly glycosylated protein with a mass of approximately 130 kDa. [9] The structure of this protein was determined by molecular cloning in 1990, when it was found out that PECAM-1 has an N-terminal domain with 574 amino acids, a transmembrane domain with 19 amino acids and a C-terminal cytoplasmic domain with 118 amino acids.