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Secondary structure and membrane localization of synthetic segments and a truncated form of the IsK (minK) protein

IsK, also referred to as minK, is a membrane protein consisting of 130 amino acids and localized mainly in epithelial cells but also in human T lymphocytes. Depending on the cRNA concentration that was injected into Xenopus oocytes, IsK and its truncated forms can induce either a K+ current alone or... Full description

Journal Title: Biochemistry 07 June 1994, Vol.33(22), pp.6966-73
Main Author: Ben-Efraim, I
Other Authors: Strahilevitz, J , Bach, D , Shai, Y
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0006-2960 ; PMID: 8204631 Version:1
Link: http://pubmed.gov/8204631
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title: Secondary structure and membrane localization of synthetic segments and a truncated form of the IsK (minK) protein
format: Article
creator:
  • Ben-Efraim, I
  • Strahilevitz, J
  • Bach, D
  • Shai, Y
subjects:
  • Potassium Channels, Voltage-Gated
  • Protein Structure, Secondary
  • Potassium Channels -- Chemistry
ispartof: Biochemistry, 07 June 1994, Vol.33(22), pp.6966-73
description: IsK, also referred to as minK, is a membrane protein consisting of 130 amino acids and localized mainly in epithelial cells but also in human T lymphocytes. Depending on the cRNA concentration that was injected into Xenopus oocytes, IsK and its truncated forms can induce either a K+ current alone or both K+ and Cl- currents [Attali et al. (1993) Nature 365, 850-852]. To obtain information on the secondary structure and the topology of IsK in a membrane-bound state, the synthesis, fluorescent-labeling, and structural and functional characterization of five polypeptides of 20-63 amino acids within the rat IsK protein were examined. The alpha-helical content of the segments, assessed in methanol using circular dichroism, suggests that both the N-terminal and transmembrane segments of IsK adopt alpha-helical structures. Binding experiments and the blue shift of 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-labeled peptides suggest that while both the alpha-helical transmembrane segment and the N-terminal...
language: eng
source:
identifier: ISSN: 0006-2960 ; PMID: 8204631 Version:1
fulltext: fulltext
issn:
  • 00062960
  • 0006-2960
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titleSecondary structure and membrane localization of synthetic segments and a truncated form of the IsK (minK) protein
creatorBen-Efraim, I ; Strahilevitz, J ; Bach, D ; Shai, Y
ispartofBiochemistry, 07 June 1994, Vol.33(22), pp.6966-73
identifierISSN: 0006-2960 ; PMID: 8204631 Version:1
subjectPotassium Channels, Voltage-Gated ; Protein Structure, Secondary ; Potassium Channels -- Chemistry
descriptionIsK, also referred to as minK, is a membrane protein consisting of 130 amino acids and localized mainly in epithelial cells but also in human T lymphocytes. Depending on the cRNA concentration that was injected into Xenopus oocytes, IsK and its truncated forms can induce either a K+ current alone or both K+ and Cl- currents [Attali et al. (1993) Nature 365, 850-852]. To obtain information on the secondary structure and the topology of IsK in a membrane-bound state, the synthesis, fluorescent-labeling, and structural and functional characterization of five polypeptides of 20-63 amino acids within the rat IsK protein were examined. The alpha-helical content of the segments, assessed in methanol using circular dichroism, suggests that both the N-terminal and transmembrane segments of IsK adopt alpha-helical structures. Binding experiments and the blue shift of 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-labeled peptides suggest that while both the alpha-helical transmembrane segment and the N-terminal...
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titleSecondary structure and membrane localization of synthetic segments and a truncated form of the IsK (minK) protein
descriptionIsK, also referred to as minK, is a membrane protein consisting of 130 amino acids and localized mainly in epithelial cells but also in human T lymphocytes. Depending on the cRNA concentration that was injected into Xenopus oocytes, IsK and its truncated forms can induce either a K+ current alone or both K+ and Cl- currents [Attali et al. (1993) Nature 365, 850-852]. To obtain information on the secondary structure and the topology of IsK in a membrane-bound state, the synthesis, fluorescent-labeling, and structural and functional characterization of five polypeptides of 20-63 amino acids within the rat IsK protein were examined. The alpha-helical content of the segments, assessed in methanol using circular dichroism, suggests that both the N-terminal and transmembrane segments of IsK adopt alpha-helical structures. Binding experiments and the blue shift of 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-labeled peptides suggest that while both the alpha-helical transmembrane segment and the N-terminal...
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abstractIsK, also referred to as minK, is a membrane protein consisting of 130 amino acids and localized mainly in epithelial cells but also in human T lymphocytes. Depending on the cRNA concentration that was injected into Xenopus oocytes, IsK and its truncated forms can induce either a K+ current alone or both K+ and Cl- currents [Attali et al. (1993) Nature 365, 850-852]. To obtain information on the secondary structure and the topology of IsK in a membrane-bound state, the synthesis, fluorescent-labeling, and structural and functional characterization of five polypeptides of 20-63 amino acids within the rat IsK protein were examined. The alpha-helical content of the segments, assessed in methanol using circular dichroism, suggests that both the N-terminal and transmembrane segments of IsK adopt alpha-helical structures. Binding experiments and the blue shift of 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-labeled peptides suggest that while both the alpha-helical transmembrane segment and the N-terminal...
pmid8204631
doi10.1021/bi00188a028
eissn15204995
date1994-06-07