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Bimolecular fluorescence complementation (also known as BiFC) is a technology typically used to validate protein interactions. It is based on the association of fluorescent protein fragments that are attached to components of the same macromolecular complex.
Biomolecules are an important element of living organisms. They are often endogenous, [2] i.e. produced within the organism, [3] but organisms usually also need exogenous biomolecules, for example certain nutrients, to survive. Biomolecules and their reactions are studied in biology and its subfields of biochemistry and molecular biology.
An example involves the conversion of the ethyl ester of 5-bromovaleric acid to the iodide: [4] EtO 2 C(CH 2) 4 Br + NaI → EtO 2 C(CH 2) 4 I + NaBr. Potassium fluoride is used for the conversion of chlorocarbons into fluorocarbons. [5] Such reactions usually employ polar solvents such as dimethyl formamide, ethylene glycol, and dimethyl ...
The kinetic order of any elementary reaction or reaction step is equal to its molecularity, and the rate equation of an elementary reaction can therefore be determined by inspection, from the molecularity. [1] The kinetic order of a complex (multistep) reaction, however, is not necessarily equal to the number of molecules involved.
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.
The bimolecular nucleophilic substitution (S N 2) is a type of reaction mechanism that is common in organic chemistry. In the S N 2 reaction, a strong nucleophile forms a new bond to an sp 3 -hybridised carbon atom via a backside attack, all while the leaving group detaches from the reaction center in a concerted (i.e. simultaneous) fashion.
The reaction mechanism of the Biginelli reaction is a series of bimolecular reactions leading to the desired dihydropyrimidinone. [14]According to a mechanism proposed by Sweet in 1973 the aldol condensation of ethylacetoacetate 1 and the aryl aldehyde is the rate-limiting step leading to the carbenium ion 2.
This reaction was the basis of Dorothy Wrinch's cyclol model of proteins. The cyclol hypothesis is the now discredited first structural model of a folded, globular protein, formulated in the 1930s. [1] It was based on the cyclol reaction of peptide bonds proposed by physicist Charles Frank in 1936, [2] in which two peptide groups are chemically ...