Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two-dimensional crystals of soluble proteins were formed at the interface between an aqueous solution of proteins and a thin organic liquid (dehydroabietylamine). Proteins were adsorbed to the interface from the aqueous side and formed a two-dimensional crystal under suitable conditions. This method offers the advantage of great surface mobility and ideal homogeneity. Furthermore, the positive charge attracted negatively charged proteins well to the interface and no denaturation of the proteins was observed. With this technique, two-dimensional crystals of ferritin, catalase, chaperonin and 50S ribosome were prepared and their structural features were determined.
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PMID:A method for 2D crystallization of soluble proteins at liquid-liquid interface. 773 20

Some proteins of E. coli are stable at temperatures significantly higher than 49 degrees C, the maximum temperature at which the organism can grow. The heat stability of such proteins would be a property which is inherent to their structures, or it might be acquired by evolution for their specialized functions. In this study, we describe the identification of 17 heat-stable proteins from E. coli. Approximately one-third of these proteins were recognized as having functions in the protection of other proteins against denaturation. These included chaperonin (GroEL and GroES), molecular chaperones (DnaK and FkpA) and peptidyl prolyl isomerases (trigger factor and FkpA). Another common feature was that five of these proteins (GroEL, GroES, Ahpc, RibH and ferritin) have been shown to form a macromolecular structure. These results indicated that the heat stability of certain proteins may have evolved for their specialized functions, allowing them to cope with harsh environments, including high temperatures.
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PMID:Proteomic analysis of heat-stable proteins in Escherichia coli. 1831 45