LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Back to previous search Search history
Advanced search

Your last searches

  1. AU=Tronin Andrey Y.
  2. AU="Singh, Jyoti"
  3. AU=Charlier Philippe
  4. AU="Thiermann, Horst"
  5. AU="Gullo, Paride"
  6. AU="Lewis, Gayle"
  7. AU=Jain Harshwardhan AU=Jain Harshwardhan
  8. AU="Gaur, Aman"
  9. AU=Huynh Thu P.
  10. AU=Giebel Clarissa
  11. AU=Laskin Daniel M

Search results

Result 1 - 5 of total 5

Search options

  1. Article ; Online: Voltage-Dependent Profile Structures of a Kv-Channel via Time-Resolved Neutron Interferometry.

    Tronin, Andrey Y / Maciunas, Lina J / Grasty, Kimberly C / Loll, Patrick J / Ambaye, Haile A / Parizzi, Andre A / Lauter, Valeria / Geragotelis, Andrew D / Freites, J Alfredo / Tobias, Douglas J / Blasie, J Kent

    Biophysical journal

    2019  Volume 117, Issue 4, Page(s) 751–766

    Abstract: Available experimental techniques cannot determine high-resolution three-dimensional structures of membrane proteins under a transmembrane voltage. Hence, the mechanism by which voltage-gated cation channels couple conformational changes within the four ... ...

    Abstract Available experimental techniques cannot determine high-resolution three-dimensional structures of membrane proteins under a transmembrane voltage. Hence, the mechanism by which voltage-gated cation channels couple conformational changes within the four voltage sensor domains, in response to either depolarizing or polarizing transmembrane voltages, to opening or closing of the pore domain's ion channel remains unresolved. Single-membrane specimens, composed of a phospholipid bilayer containing a vectorially oriented voltage-gated K
    MeSH term(s) Interferometry ; Ion Channel Gating ; Lipid Bilayers/chemistry ; Membrane Potentials ; Molecular Dynamics Simulation ; Neutrons ; Potassium Channels, Voltage-Gated/chemistry ; Protein Domains
    Chemical Substances Lipid Bilayers ; Potassium Channels, Voltage-Gated
    Language English
    Publishing date 2019-07-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2019.07.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 235: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 2: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article: Direct Evidence of Conformational Changes Associated with Voltage Gating in a Voltage Sensor Protein by Time-Resolved X-ray/Neutron Interferometry

    Tronin, Andrey Y / Blasie J. Kent / Freites J. Alfredo / Kuzmenko Ivan / Lauter Valeria / Nordgren C. Erik / Strzalka Joseph W / Tobias Douglas J / Worcester David L

    Langmuir. 2014 Apr. 29, v. 30, no. 16

    2014  

    Abstract: The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na⁺, K⁺) channels central to neurological signal transmission can function as a distinct module. When linked to an otherwise voltage-insensitive, ion-selective membrane pore, the VSD ... ...

    Abstract The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na⁺, K⁺) channels central to neurological signal transmission can function as a distinct module. When linked to an otherwise voltage-insensitive, ion-selective membrane pore, the VSD imparts voltage sensitivity to the channel. Proteins homologous with the VSD have recently been found to function themselves as voltage-gated proton channels or to impart voltage sensitivity to enzymes. Determining the conformational changes associated with voltage gating in the VSD itself in the absence of a pore domain thereby gains importance. We report the direct measurement of changes in the scattering-length density (SLD) profile of the VSD protein, vectorially oriented within a reconstituted phospholipid bilayer membrane, as a function of the transmembrane electric potential by time-resolved X-ray and neutron interferometry. The changes in the experimental SLD profiles for both polarizing and depolarizing potentials with respect to zero potential were found to extend over the entire length of the isolated VSD’s profile structure. The characteristics of the changes observed were in qualitative agreement with molecular dynamics simulations of a related membrane system, suggesting an initial interpretation of these changes in terms of the VSD’s atomic-level 3-D structure.
    Keywords cations ; electric power ; enzymes ; interferometry ; molecular dynamics ; neutrons ; phospholipids ; potassium ; proteins ; sodium ; X-radiation
    Language English
    Dates of publication 2014-0429
    Size p. 4784-4796.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021%2Fla500560w
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Mechanism of interaction between the general anesthetic halothane and a model ion channel protein, I: Structural investigations via X-ray reflectivity from Langmuir monolayers.

    Strzalka, Joseph / Liu, Jing / Tronin, Andrey / Churbanova, Inna Y / Johansson, Jonas S / Blasie, J Kent

    Biophysical journal

    2009  Volume 96, Issue 10, Page(s) 4164–4175

    Abstract: We previously reported the synthesis and structural characterization of a model membrane protein comprised of an amphiphilic 4-helix bundle peptide with a hydrophobic domain based on a synthetic ion channel and a hydrophilic domain with designed cavities ...

    Abstract We previously reported the synthesis and structural characterization of a model membrane protein comprised of an amphiphilic 4-helix bundle peptide with a hydrophobic domain based on a synthetic ion channel and a hydrophilic domain with designed cavities for binding the general anesthetic halothane. In this work, we synthesized an improved version of this halothane-binding amphiphilic peptide with only a single cavity and an otherwise identical control peptide with no such cavity, and applied x-ray reflectivity to monolayers of these peptides to probe the distribution of halothane along the length of the core of the 4-helix bundle as a function of the concentration of halothane. At the moderate concentrations achieved in this study, approximately three molecules of halothane were found to be localized within a broad symmetric unimodal distribution centered about the designed cavity. At the lowest concentration achieved, of approximately one molecule per bundle, the halothane distribution became narrower and more peaked due to a component of approximately 19A width centered about the designed cavity. At higher concentrations, approximately six to seven molecules were found to be uniformly distributed along the length of the bundle, corresponding to approximately one molecule per heptad. Monolayers of the control peptide showed only the latter behavior, namely a uniform distribution along the length of the bundle irrespective of the halothane concentration over this range. The results provide insight into the nature of such weak binding when the dissociation constant is in the mM regime, relevant for clinical applications of anesthesia. They also demonstrate the suitability of both the model system and the experimental technique for additional work on the mechanism of general anesthesia, some of it presented in the companion parts II and III under this title.
    MeSH term(s) Amino Acid Sequence ; Anesthetics, General/chemistry ; Anesthetics, General/metabolism ; Halothane/chemistry ; Halothane/metabolism ; Ion Channels/chemical synthesis ; Ion Channels/chemistry ; Ion Channels/metabolism ; Molecular Sequence Data ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/metabolism ; Protein Binding ; X-Rays
    Chemical Substances Anesthetics, General ; Ion Channels ; Peptides ; Halothane (UQT9G45D1P)
    Language English
    Publishing date 2009-01-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2009.01.053
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 235: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 2: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Direct evidence of conformational changes associated with voltage gating in a voltage sensor protein by time-resolved X-ray/neutron interferometry.

    Tronin, Andrey Y / Nordgren, C Erik / Strzalka, Joseph W / Kuzmenko, Ivan / Worcester, David L / Lauter, Valeria / Freites, J Alfredo / Tobias, Douglas J / Blasie, J Kent

    Langmuir : the ACS journal of surfaces and colloids

    2014  Volume 30, Issue 16, Page(s) 4784–4796

    Abstract: The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na(+), K(+)) channels central to neurological signal transmission can function as a distinct module. When linked to an otherwise voltage-insensitive, ion-selective membrane pore, the VSD ... ...

    Abstract The voltage sensor domain (VSD) of voltage-gated cation (e.g., Na(+), K(+)) channels central to neurological signal transmission can function as a distinct module. When linked to an otherwise voltage-insensitive, ion-selective membrane pore, the VSD imparts voltage sensitivity to the channel. Proteins homologous with the VSD have recently been found to function themselves as voltage-gated proton channels or to impart voltage sensitivity to enzymes. Determining the conformational changes associated with voltage gating in the VSD itself in the absence of a pore domain thereby gains importance. We report the direct measurement of changes in the scattering-length density (SLD) profile of the VSD protein, vectorially oriented within a reconstituted phospholipid bilayer membrane, as a function of the transmembrane electric potential by time-resolved X-ray and neutron interferometry. The changes in the experimental SLD profiles for both polarizing and depolarizing potentials with respect to zero potential were found to extend over the entire length of the isolated VSD's profile structure. The characteristics of the changes observed were in qualitative agreement with molecular dynamics simulations of a related membrane system, suggesting an initial interpretation of these changes in terms of the VSD's atomic-level 3-D structure.
    MeSH term(s) Interferometry/methods ; Ion Channel Gating/physiology ; Ion Channels/chemistry ; Lipid Bilayers/chemistry ; Neutrons ; Phospholipids/chemistry ; X-Rays
    Chemical Substances Ion Channels ; Lipid Bilayers ; Phospholipids
    Language English
    Publishing date 2014-04-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/la500560w
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: Monolayers of a model anesthetic-binding membrane protein: formation, characterization, and halothane-binding affinity.

    Churbanova, Inna Y / Tronin, Andrey / Strzalka, Joseph / Gog, Thomas / Kuzmenko, Ivan / Johansson, Jonas S / Blasie, J Kent

    Biophysical journal

    2006  Volume 90, Issue 9, Page(s) 3255–3266

    Abstract: hbAP0 is a model membrane protein designed to possess an anesthetic-binding cavity in its hydrophilic domain and a cation channel in its hydrophobic domain. Grazing incidence x-ray diffraction shows that hbAP0 forms four-helix bundles that are ... ...

    Abstract hbAP0 is a model membrane protein designed to possess an anesthetic-binding cavity in its hydrophilic domain and a cation channel in its hydrophobic domain. Grazing incidence x-ray diffraction shows that hbAP0 forms four-helix bundles that are vectorially oriented within Langmuir monolayers at the air-water interface. Single monolayers of hbAP0 on alkylated solid substrates would provide an optimal system for detailed structural and dynamical studies of anesthetic-peptide interaction via x-ray and neutron scattering and polarized spectroscopic techniques. Langmuir-Blodgett and Langmuir-Schaeffer deposition and self-assembly techniques were used to form single monolayer films of the vectorially oriented peptide hbAP0 via both chemisorption and physisorption onto suitably alkylated solid substrates. The films were characterized by ultraviolet absorption, ellipsometry, circular dichroism, and polarized Fourier transform infrared spectroscopy. The alpha-helical secondary structure of the peptide was retained in the films. Under certain conditions, the average orientation of the helical axis was inclined relative to the plane of the substrate, approaching perpendicular in some cases. The halothane-binding affinity of the vectorially oriented hbAP0 peptide in the single monolayers, with the volatile anesthetic introduced into the moist vapor environment of the monolayer, was found to be similar to that for the detergent-solubilized peptide.
    MeSH term(s) Adsorption ; Amino Acid Sequence ; Anesthetics/metabolism ; Anesthetics, Inhalation/chemistry ; Anesthetics, Inhalation/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Circular Dichroism ; Halothane/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Spectrophotometry, Infrared
    Chemical Substances Anesthetics ; Anesthetics, Inhalation ; Carrier Proteins ; Membrane Proteins ; Halothane (UQT9G45D1P)
    Language English
    Publishing date 2006-05-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1529/biophysj.105.072348
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 235: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 2: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top