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Late embryogenesis abundant proteins (LEA proteins) are proteins in plants, and some bacteria and invertebrates, that protect against protein aggregation due to desiccation or osmotic stresses associated with low temperature. [1] [2] [3] LEA proteins were initially discovered accumulating late in embryogenesis of cotton seeds. [4]
Photosynthetic reaction centre proteins are main protein components of photosynthetic reaction centres (RCs) of bacteria and plants. They are transmembrane proteins embedded in the chloroplast thylakoid or bacterial cell membrane. Plants, algae, and cyanobacteria have one type of PRC for each of its two photosystems.
Plant seed proteins are small hydrophilic proteins. They represent a subset of late embryogenesis abundant proteins, of Dure subfamily D-19 or Bray group 1.These proteins contain from 73 to 153 amino acid residues and may play a role in equipping the seed for survival, maintaining a minimal level of hydration in the dry organism and preventing the denaturation of cytoplasmic components.
Plastocyanin is a copper-containing protein that mediates electron-transfer. It is found in a variety of plants, where it participates in photosynthesis. The protein is a prototype of the blue copper proteins, a family of intensely blue-colored metalloproteins. Specifically, it falls into the group of small type I blue copper proteins called ...
In photoinhibition studies, repair is often stopped by applying an antibiotic (lincomycin or chloramphenicol) to plants or cyanobacteria, which blocks protein synthesis in the chloroplast. Protein synthesis occurs only in an intact sample, so lincomycin is not needed when photoinhibition is measured from isolated membranes. [27]
It is a large and functionally immensely diverse 'superfamily' of proteins, numbering in the thousands, that have a common origin and whose evolution can be followed from bacteria to eukaryotes including animals and higher plants. "Cupins" are the most functionally diverse protein superfamily occurring in all spermatophytes (seed-bearing plants).
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Two tyrosines separated by a single amino acid, typically valine or another tyrosine, form a short intra-molecular diphenylether crosslink. [11] This can be crosslinked further by the enzyme extensin peroxidase [12] [13] [14] to form an inter-molecular bridge between extensin molecules and thus form networks and sheets.