Chaperone of endosialidaseThis is the very C-terminal, chaperone, doma translation - Chaperone of endosialidaseThis is the very C-terminal, chaperone, doma Indonesian how to say

Chaperone of endosialidaseThis is t

Chaperone of endosialidase
This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and presumably bind to DNA.
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Pengawal endosialidaseIni adalah sangat C-terminal, pengawal, domain Bacteriofag protein endosialidase. Ini rilis itu sendiri, melalui dyad Serin-lisin N-ujung, dari sisa akhir-ekor-lonjakan. Pembelahan terjadi setelah Treonina yang residu akhir akhir-ekor-spike Keluarga, pfam12219. Endosialidase protein membentuk molekul homotrimeric di bacteriophages. Dyad katalitik memungkinkan bagian ini molekul untuk diurai dari daerah N-terminal lebih seperti yang kedua dapat melipat dan agaknya mengikat DNA.
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Pendamping dari endosialidase
ini adalah sangat C-terminal, pendamping, domain dari endosialidase protein bakteriofag. Ia melepaskan sendiri, melalui angka dua serin-lisin pada N-terminus, dari sisa akhir-ekor-spike. Pembelahan terjadi setelah treonin yang merupakan residu akhir dari keluarga End-ekor-lonjakan, pfam12219. Protein endosialidase membentuk molekul homotrimeric di bakteriofag. The angka dua katalitik memungkinkan ini bagian dari molekul yang akan dibelah dari lebih daerah N-terminal tersebut bahwa yang terakhir dapat melipat dan mungkin mengikat DNA.
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