Hydrophobicity of AgrD1



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送交者: 桂铭 于 2006-1-24, 02:49:39:

回答: More Speculation on Dr. Qiu’s Paper 由 Godfather 于 2006-1-23, 18:01:32:

AgrD1 YSTCDFIM
Highly hydrophobic amino acid residues: F, I, M, C, Y

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J. Membrane Biol. 157, 27–37 (1997):
channel formation (C-terminal domain). Near the carboxyl end of the channel forming domain is a hydrophobic segment, which is present in all the channel-forming colicins; in colicin Ia
it is 40 residues long (residues 573–612) [12]. The hydrophobic segment forms an a-helical hairpin in the
crystal structures of colicins A, E1, and Ia [18, 24, 25]. It is thought that this helical hairpin structure is preserved when the colicin changes its conformation to form a transmembrane channel.
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With 5 very hydrophobic residues out of 8 residues added to the C-terminal segment, how much the hydrophobic property of C-terminal domain will be changed?



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