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Leucine incorporation is used as a measure of protein synthesis in aquatic bacteria communities. [39] Radio-labeled leucine is added to samples, and its accumulation into proteins, the hot trichloroacetic acid (CA)-insoluble parts of the cell is determined. [39] The samples are then collected on membrane filter. [39]
In this example, the labeled protein has the same abundance in both samples (ratio 1). Stable isotope labeling by/with amino acids in cell culture (SILAC) is a technique based on mass spectrometry that detects differences in protein abundance among samples using non-radioactive isotopic labeling.
A bacterial initiation factor (IF) is a protein that stabilizes the initiation complex for polypeptide translation. Translation initiation is essential to protein synthesis and regulates mRNA translation fidelity and efficiency in bacteria. [1] The 30S ribosomal subunit, initiator tRNA, and mRNA form an initiation complex for elongation. [2]
Protein methods are the techniques used to study proteins.There are experimental methods for studying proteins (e.g., for detecting proteins, for isolating and purifying proteins, and for characterizing the structure and function of proteins, [1] often requiring that the protein first be purified).
BCA protein assay in a 96 well plate. The bicinchoninic acid assay (BCA assay), also known as the Smith assay, after its inventor, Paul K. Smith at the Pierce Chemical Company, [1] now part of Thermo Fisher Scientific, is a biochemical assay for determining the total concentration of protein in a solution (0.5 μg/mL to 1.5 mg/mL), similar to Lowry protein assay, Bradford protein assay or ...
Several different vendors offer SPR-based devices. Best known are Biacore instruments which were the first commercially available. Dual polarisation interferometry (DPI) can be used to measure protein–protein interactions. DPI provides real-time, high-resolution measurements of molecular size, density and mass.
Bacterial display (or bacteria display or bacterial surface display) is a protein engineering technique used for in vitro protein evolution. Libraries of polypeptides displayed on the surface of bacteria can be screened using flow cytometry or iterative selection procedures (biopanning).
For example, a DNA sequence for a protein of interest could be cloned or subcloned into a high copy-number plasmid containing the lac (often LacUV5) promoter, which is then transformed into the bacterium E. coli. Addition of IPTG (a lactose analog) activates the lac promoter and causes the bacteria to express the protein of interest. [2]