Literature DB >> 2423148

Open channel noise. II. A test for coupling between current fluctuations and conformational transitions in the acetylcholine receptor.

F J Sigworth.   

Abstract

The first paper of this series demonstrated that the open-channel currents in the acetylcholine receptors in cultured rat muscle show fluctuations on a time scale of approximately 1 ms. In this paper the hypothesis is tested that these fluctuations are coupled to the gating mechanism that opens and closes the channel. Such a coupling could arise if the channel current and the energy barrier for gating transitions both showed fluctuations having a common origin such as a motion of part of the receptor molecule. A test for coupled fluctuations is made by averaging approximately 1,000 channel opening or closing transitions to search for the small relaxation in the current that is predicted. At a resolution of approximately 1% of the single-channel current amplitude, no such relaxation is observed. It is concluded that any coupled fluctuations are small; fluctuations in the energy barrier for the open-closed conformational transition must be smaller than about 0.3 kT.

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Year:  1986        PMID: 2423148      PMCID: PMC1329684          DOI: 10.1016/S0006-3495(86)83732-8

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  3 in total

1.  Open channel noise. I. Noise in acetylcholine receptor currents suggests conformational fluctuations.

Authors:  F J Sigworth
Journal:  Biophys J       Date:  1985-05       Impact factor: 4.033

2.  Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches.

Authors:  O P Hamill; A Marty; E Neher; B Sakmann; F J Sigworth
Journal:  Pflugers Arch       Date:  1981-08       Impact factor: 3.657

3.  Flickering of a nicotinic ion channel to a subconductance state.

Authors:  A Auerbach; F Sachs
Journal:  Biophys J       Date:  1983-04       Impact factor: 4.033

  3 in total
  16 in total

1.  Determining the activation time course of synaptic AMPA receptors from openings of colocalized NMDA receptors.

Authors:  I C Kleppe; H P Robinson
Journal:  Biophys J       Date:  1999-09       Impact factor: 4.033

2.  Single channel properties of P2X2 purinoceptors.

Authors:  S Ding; F Sachs
Journal:  J Gen Physiol       Date:  1999-05       Impact factor: 4.086

3.  Characterization of inositol-1,4,5-trisphosphate-gated channels in the plasma membrane of rat olfactory neurons.

Authors:  F W Lischka; M M Zviman; J H Teeter; D Restrepo
Journal:  Biophys J       Date:  1999-03       Impact factor: 4.033

4.  Open channel noise. V. Fluctuating barriers to ion entry in gramicidin A channels.

Authors:  S H Heinemann; F J Sigworth
Journal:  Biophys J       Date:  1990-03       Impact factor: 4.033

5.  Extracting dwell time sequences from processive molecular motor data.

Authors:  Lorin S Milescu; Ahmet Yildiz; Paul R Selvin; Frederick Sachs
Journal:  Biophys J       Date:  2006-08-11       Impact factor: 4.033

6.  Statistical assessment of change point detectors for single molecule kinetic analysis.

Authors:  Sean P Parsons; Jan D Huizinga
Journal:  J Membr Biol       Date:  2013-05-08       Impact factor: 1.843

7.  The conductance of the muscle nicotinic receptor channel changes rapidly upon gating.

Authors:  D J Maconochie; G H Fletcher; J H Steinbach
Journal:  Biophys J       Date:  1995-02       Impact factor: 4.033

8.  Open channel noise. III. High-resolution recordings show rapid current fluctuations in gramicidin A and four chemical analogues.

Authors:  F J Sigworth; D W Urry; K U Prasad
Journal:  Biophys J       Date:  1987-12       Impact factor: 4.033

9.  Internal motions in proteins and gating kinetics of ionic channels.

Authors:  P Läuger
Journal:  Biophys J       Date:  1988-06       Impact factor: 4.033

10.  Gating transitions in bacterial ion channels measured at 3 microns resolution.

Authors:  George Shapovalov; Henry A Lester
Journal:  J Gen Physiol       Date:  2004-08       Impact factor: 4.086

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