Search results
Results From The WOW.Com Content Network
In biochemistry, the molar absorption coefficient of a protein at 280 nm depends almost exclusively on the number of aromatic residues, particularly tryptophan, and can be predicted from the sequence of amino acids. [6] Similarly, the molar absorption coefficient of nucleic acids at 260 nm can be predicted given the nucleotide sequence.
TEV protease (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV). [1] It is a member of the PA clan of chymotrypsin-like proteases. [2]
Sequence reads are mapped to splice graphs that unambiguously quantify the inclusion level of each exon and splice junction. The graphs are then traversed to predict the protein isoforms that are likely to result from the observed exon and splice junction reads.
CRM197 is used as a carrier protein in a number of approved conjugate vaccines. Hibtiter™, a vaccine to protect against Haemophilus influenzae type b, approved by the FDA in 1990, was the first conjugate vaccine to use CRM197 (the vaccine was discontinued in 2007).
The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [ 2 ] spectroscopic analytical procedure used to measure the concentration of protein in a solution.
The photophysical properties of the FbFPs are determined by the chromophore itself and its chemical surrounding in the protein. The extinction coefficient (ε) is around 14.200 M −1 cm −1 at 450 nm for all described FbFPs, which is slightly higher than that of free FMN (ε = 12.200 M −1 cm −1 [10]).
At a wavelength of 260 nm, the average extinction coefficient for double-stranded DNA is 0.020 (μg/mL) −1 cm −1, for single-stranded DNA it is 0.027 (μg/mL) −1 cm −1, for single-stranded RNA it is 0.025 (μg/mL) −1 cm −1 and for short single-stranded oligonucleotides it is dependent on the length and base composition.
The Warburg–Christian method is an ultraviolet spectroscopic protein and nucleic acid assay method based on the absorbance of UV light at 260 nm and 280 nm wavelengths. . Proteins generally absorb light at 280 nanometers due to the presence of tryptophan and ty