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On the nature of the unfolded intermediate in the in vitro transition of the colicin E1 channel domain from the aqueous to the membrane phase.

The transition of the colicin E1 channel polypeptide from a water-soluble to membrane-bound state occurs in vitro at acid pH values that are associated with an unfolded channel structure whose properties qualitatively resemble those of a "molten globule," or "compact unfolded," i...

詳細記述

保存先:
書誌詳細
主要な著者: Schendel, S. L., Cramer, W. A.
フォーマット: Artigo
言語:Inglês
出版事項: Cold Spring Harbor Laboratory Press 1994
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142766/
https://ncbi.nlm.nih.gov/pubmed/7756984
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