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Constraints imposed by protease accessibility on the trans-membrane and surface topography of the colicin E1 ion channel.

The surface topography of a 190-residue COOH-terminal colicin E1 channel peptide (NH2-Met 333-Ile 522-COOH) bound to uniformly sized 0.2-micron liposomes was probed by accessibility of the peptide to proteases in order (1) to determine whether the channel structure contains trans-membrane segments i...

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Main Authors: Zhang, Y. L., Cramer, W. A.
格式: Artigo
語言:Inglês
出版: Cold Spring Harbor Laboratory Press 1992
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142128/
https://ncbi.nlm.nih.gov/pubmed/1284805
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