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MMA is a raw material for the manufacture of other methacrylates. These derivatives include ethyl methacrylate (EMA), butyl methacrylate (BMA) and 2-ethyl hexyl methacrylate (2-EHMA). Methacrylic acid (MAA) is used as a chemical intermediate as well as in the manufacture of coating polymers, construction chemicals and textile applications.
The BChl a molecules are depicted in green, the central magnesium atom in red and the protein in grey ("cartoons" representation). Each monomer contains bacteriochlorophylls. The Fenna–Matthews–Olson (FMO) complex is a water-soluble complex and was the first pigment-protein complex (PPC) to be structure analyzed by x-ray spectroscopy. [2]
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. [5] It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES.
A protein structure database is a database that is modeled around the various experimentally determined protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way.
The structure of the Bacterial Microcompartment shell. The first structure of a BMC shell, determined by X-ray crystallography and cryo-electron microscopy, [1] contains representatives of each of the shell protein types: BMC-P, BMC-H and BMC-T, in both its trimer (upper right) and dimer of trimer (lower right), forms.
Methylmalonic acid (MMA) is a chemical compound from the group of dicarboxylic acids. It consists of the basic structure of malonic acid and also carries a methyl group . The salts of methylmalonic acid are called methylmalonates .
Non-specific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates on DNA. MutS is a modular protein with a complex structure, [5] and is composed of:
In addition to protein L, other immunoglobulin-binding bacterial proteins such as protein A, protein G and protein A/G are all commonly used to purify, immobilize or detect immunoglobulins. Each of these immunoglobulin-binding proteins has a different antibody binding profile in terms of the portion of the antibody that is recognized and the ...