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Phage P22 Tailspike Protein : ウィキペディア英語版 | Phage P22 Tailspike Protein
The tailspike protein (P22TSP) of Enterobacteria phage P22 mediates the recognition and adhesion between the bacteriophage and the surface of ''Salmonella enterica'' cells. It is anchored within the viral coat and recognizes the O-antigen portion of the lipopolysaccharide (LPS) on the outer-membrane of Gram-negative bacteria. It possesses endoglycanase activity, serving to shorten the length of the O-antigen during infection. ==History==
The initial interest in tailspike proteins was in the study of the effect the mutations on protein folding. Some mutations affect the folding efficiency of the protein but have no effect on the final native structure. Other mutations have been identified that lead to a temperature sensitive phenotype. Reconstitution experiments have demonstrated that the in vitro folding process closely mirrors the in vivo folding pathway.〔 It has been further been demonstrated that folding yields in vitro decrease strongly with increasing temperature.
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Phage P22 Tailspike Protein」の詳細全文を読む
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