| 书目名称 | Proteins |
| 副标题 | Membrane Binding and |
| 编辑 | Gregor Anderluh,Jeremy Lakey |
| 视频video | |
| 概述 | Novel structures and biophysical studies on proteins.Includes a comparison of the properties of membrane channels formed by amyloid proteins and pore forming toxins.Gives comprehensive overview of wha |
| 丛书名称 | Advances in Experimental Medicine and Biology |
| 图书封面 |  |
| 描述 | Formation of transmembrane pores is a very effective way of killing cells. It is thus not surprising that many bacterial and eukaryotic toxic agents are pore-forming proteins. Pore formation in a target membrane is a complex process composed of several steps; proteins need to attach to the lipid membrane, possibly aggregate in the plane of the membrane and finally form a pore by inserting part of the polypeptide chain across the lipid bilayer. Structural information about toxins at each stage is indispensible for the biochemical and molecular biological studies that aim to - derstand how pores are formed at the molecular level. There are currently only two Staphylococcus aureus and hemolysin E from Escherichia coli. Therefore, what we know about these proteins was obtained over many years of intense experimentation. We have nevertheless, in the last couple of years, witnessed a significant rise in structural information on the soluble forms of pore-forming proteins. Surprisingly, many unexpected similarities with other proteins were noted, despite extremely low or insignificant sequence similarity. It appears that lipid membrane binding and formation of transmembrane channels is ac |
| 出版日期 | Book 2010 |
| 关键词 | Anderluh; Lakey; Pore; membrane; peptides; protein; proteins |
| 版次 | 1 |
| doi | https://doi.org/10.1007/978-1-4419-6327-7 |
| isbn_softcover | 978-1-4939-4098-1 |
| isbn_ebook | 978-1-4419-6327-7Series ISSN 0065-2598 Series E-ISSN 2214-8019 |
| issn_series | 0065-2598 |
| copyright | The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines |
发表于 2025-3-21 19:04:19
