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  Structure of the inactivating gate from the Shaker voltage gated K+ channel analyzed by NMR spectroscopy

Schott, M. K., Antz, C., Frank, R., Ruppersberg, J. P., & Kalbitzer, H. R. (1998). Structure of the inactivating gate from the Shaker voltage gated K+ channel analyzed by NMR spectroscopy. European Biophysics Journal, 27(2), 99-104. doi:10.1007/s002490050115.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-77DF-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-77E0-4
Genre: Journal Article
Alternative Title : Structure of the inactivating gate from the Shaker voltage gated K+ channel analyzed by NMR spectroscopy

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EurBiophysJ_27_1998_99.pdf (Any fulltext), 345KB
 
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 Creators:
Schott, Markus K.1, Author              
Antz, Christof1, Author              
Frank, Rainer, Author
Ruppersberg, J. Peter2, Author              
Kalbitzer, Hans Robert1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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Free keywords: Shaker · Potassium-channel · NMR · Structure
 Abstract: Rapid inactivation of voltage-gated K+ (Kv) channels is mediated by an N-terminal domain (inactivating ball domain) which blocks the open channel from the cytoplasmic side. Inactivating ball domains of various Kv channels are also biologically active when synthesized separately and added as a peptide to the solution. Synthetic inactivating ball domains from different Kv channels with hardly any sequence homology mediate quite similar effects even on unrelated Kv channel subtypes whose inactivation domain has been deleted. The solution structure of the inactivating ball peptide from Shaker (Sh-P22) was analyzed with NMR spectroscopy. The NMR data indicate a non-random structure in an aqueous environment. However, while other inactivating ball peptides showed well-defined three-dimensional structures under these conditions, Sh-P22 does not have a unique, compactly folded structure in solution.

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Language(s): eng - English
 Dates: 1997-08-251997-11-071998
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: European Biophysics Journal
Source Genre: Journal
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Publ. Info: Berlin : Springer
Pages: - Volume / Issue: 27 (2) Sequence Number: - Start / End Page: 99 - 104 Identifier: ISSN: 0175-7571
CoNE: https://pure.mpg.de/cone/journals/resource/954925487773_1