We are analyzing https://link.springer.com/article/10.1007/bf01901011.

Title:
Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9 | The Journal of Membrane Biology
Description:
Single-channel analysis of electrical fluctuations induced in planar bilayer membranes by the purified human complement proteins C5b6, C7, C8, and C9 have been analyzed. Reconstitution experiments with lipid bilayer membranes showed that the C5b-9 proteins formed pores only if all proteins were present at one side of the membrane. The complement pores had an average single-channel conductance of 3.1 nS at 0.15m KCl. The histogram of the complement pores suggested a substantial variation of the size of the single channel. The linear relationship between single-channel conductance at fixed ionic strength and the aqueous mobility of the ions in the bulk aqueous phase indicated that the ions move inside the complement pore in a manner similar to the way they move in the aqueous phase. The minimum diameter of the pores as judged from the conductance data is approximately 3 nm. The complement channels showed no apparent voltage control or regulation up to transmembrane potentials of 100 mV. At neutral pH the pore is three to four times more permeable for alkali ions than for chloride, which may be explained by the existence of fixed negatively charged groups in or near the pore. The significance of these observations to current molecular models of the membrane lesion formed by these cytolytic serum proteins is considered.
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Keywords {🔍}

google, scholar, complement, pubmed, membrane, article, proteins, membranes, sims, lipid, bilayer, benz, channels, protein, analysis, conductance, pores, immunol, acad, sci, usa, singlechannel, wiedmer, pore, formation, biophys, acta, biol, natl, privacy, cookies, content, journal, research, induced, transmembrane, access, complex, mayer, data, publish, search, human, formed, lesion, attack, porin, mechanism, information, log,

Topics {✒️}

ion-permeable membrane channels month download article/chapter single-channel currents induced thrombosis-hematology research program average single-channel conductance antibody-coated cell membranes trans-membrane channels membrane channels formed c8-binding capacity functions c8/c9 binding required membrane potential membrane biology aims complement channels showed increased ion permeability conductance fluctuations induced antibody-antigen-complement action membrane attack complex lipid bilayer membranes single-channel conductance membrane leak generated membrane-derived protein bilayer membranes induced privacy choices/manage cookies membrane-bound complex cytolytic membrane lesion c5b-9 membrane lesion open channel noise planar bilayer membranes membrane lesion formed complement proteins c5b-9 complement proteins c5b-8 electrical fluctuations induced functional membrane damage full article pdf terminal complement proteins step conductance increases black lipid membranes single-channel analysis cytolytic serum proteins poly-c9 channels individual c5b-9 complexes complement complex c5b-9 pore forming activity complement protein c9 related subjects complement-damaged membranes article benz c9-related heterogeneity european economic area apparent voltage control

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         headline:Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9
         description:Single-channel analysis of electrical fluctuations induced in planar bilayer membranes by the purified human complement proteins C5b6, C7, C8, and C9 have been analyzed. Reconstitution experiments with lipid bilayer membranes showed that the C5b-9 proteins formed pores only if all proteins were present at one side of the membrane. The complement pores had an average single-channel conductance of 3.1 nS at 0.15m KCl. The histogram of the complement pores suggested a substantial variation of the size of the single channel. The linear relationship between single-channel conductance at fixed ionic strength and the aqueous mobility of the ions in the bulk aqueous phase indicated that the ions move inside the complement pore in a manner similar to the way they move in the aqueous phase. The minimum diameter of the pores as judged from the conductance data is approximately 3 nm. The complement channels showed no apparent voltage control or regulation up to transmembrane potentials of 100 mV. At neutral pH the pore is three to four times more permeable for alkali ions than for chloride, which may be explained by the existence of fixed negatively charged groups in or near the pore. The significance of these observations to current molecular models of the membrane lesion formed by these cytolytic serum proteins is considered.
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      headline:Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9
      description:Single-channel analysis of electrical fluctuations induced in planar bilayer membranes by the purified human complement proteins C5b6, C7, C8, and C9 have been analyzed. Reconstitution experiments with lipid bilayer membranes showed that the C5b-9 proteins formed pores only if all proteins were present at one side of the membrane. The complement pores had an average single-channel conductance of 3.1 nS at 0.15m KCl. The histogram of the complement pores suggested a substantial variation of the size of the single channel. The linear relationship between single-channel conductance at fixed ionic strength and the aqueous mobility of the ions in the bulk aqueous phase indicated that the ions move inside the complement pore in a manner similar to the way they move in the aqueous phase. The minimum diameter of the pores as judged from the conductance data is approximately 3 nm. The complement channels showed no apparent voltage control or regulation up to transmembrane potentials of 100 mV. At neutral pH the pore is three to four times more permeable for alkali ions than for chloride, which may be explained by the existence of fixed negatively charged groups in or near the pore. The significance of these observations to current molecular models of the membrane lesion formed by these cytolytic serum proteins is considered.
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      dateModified:
      pageStart:37
      pageEnd:45
      sameAs:https://doi.org/10.1007/BF01901011
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         membrane pore
         membrane conductance
         Biochemistry
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         Human Physiology
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