Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Carsten Zeilinger
  • Oliver Enders
  • Hans-Albert Kolb
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)100-107
Seitenumfang8
FachzeitschriftCONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES
Jahrgang2001
AusgabenummerVol.10(13)
PublikationsstatusVeröffentlicht - 19 März 2001

Abstract

The atomic force microscope allows to image biological samples in their native environment. But the identification and the topography of individual randomly distributed membrane proteins is still a challenge. We used membranes of isolated vacuoles of barley mesophyll cells. Images at low resolution indicate that vacuoles spontaneously attach, rupture and finally adsorb completely as planar membrane to mica. Height profiles indicate that the membrane at the peripheral boundary exposes the extravacuolar surface to the scanning tip. At molecular resolution a template matching correlation algorithm was used to identify the most abundant membrane protein, the vacuolar H+-ATPase by the characteristic extravacuolar head of the transport molecule. The data indicate the possibility to analyse single randomly distributed membrane proteins in their native environment with the knowledge of a suitable template.

Fachgebiet (basierend auf ÖFOS 2012)

Zitieren

Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm. / Zeilinger, Carsten; Enders, Oliver; Kolb, Hans-Albert.
in: CONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES, Jahrgang 2001, Nr. Vol.10(13), 19.03.2001, S. 100-107.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Zeilinger, C, Enders, O & Kolb, H-A 2001, 'Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm', CONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES, Jg. 2001, Nr. Vol.10(13), S. 100-107.
Zeilinger, C., Enders, O., & Kolb, H.-A. (2001). Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm. CONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES, 2001(Vol.10(13)), 100-107.
Zeilinger C, Enders O, Kolb HA. Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm. CONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES. 2001 Mär 19;2001(Vol.10(13)):100-107.
Zeilinger, Carsten ; Enders, Oliver ; Kolb, Hans-Albert. / Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm. in: CONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES. 2001 ; Jahrgang 2001, Nr. Vol.10(13). S. 100-107.
Download
@article{51080d11083f4d5fa18454305c775483,
title = "Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm",
abstract = "The atomic force microscope allows to image biological samples in their native environment. But the identification and the topography of individual randomly distributed membrane proteins is still a challenge. We used membranes of isolated vacuoles of barley mesophyll cells. Images at low resolution indicate that vacuoles spontaneously attach, rupture and finally adsorb completely as planar membrane to mica. Height profiles indicate that the membrane at the peripheral boundary exposes the extravacuolar surface to the scanning tip. At molecular resolution a template matching correlation algorithm was used to identify the most abundant membrane protein, the vacuolar H+-ATPase by the characteristic extravacuolar head of the transport molecule. The data indicate the possibility to analyse single randomly distributed membrane proteins in their native environment with the knowledge of a suitable template.",
author = "Carsten Zeilinger and Oliver Enders and Hans-Albert Kolb",
year = "2001",
month = mar,
day = "19",
language = "English",
volume = "2001",
pages = "100--107",
number = "Vol.10(13)",

}

Download

TY - JOUR

T1 - Identification of Membrane Proteins imaged by Atomic force microscopy using a template matching algorithm

AU - Zeilinger, Carsten

AU - Enders, Oliver

AU - Kolb, Hans-Albert

PY - 2001/3/19

Y1 - 2001/3/19

N2 - The atomic force microscope allows to image biological samples in their native environment. But the identification and the topography of individual randomly distributed membrane proteins is still a challenge. We used membranes of isolated vacuoles of barley mesophyll cells. Images at low resolution indicate that vacuoles spontaneously attach, rupture and finally adsorb completely as planar membrane to mica. Height profiles indicate that the membrane at the peripheral boundary exposes the extravacuolar surface to the scanning tip. At molecular resolution a template matching correlation algorithm was used to identify the most abundant membrane protein, the vacuolar H+-ATPase by the characteristic extravacuolar head of the transport molecule. The data indicate the possibility to analyse single randomly distributed membrane proteins in their native environment with the knowledge of a suitable template.

AB - The atomic force microscope allows to image biological samples in their native environment. But the identification and the topography of individual randomly distributed membrane proteins is still a challenge. We used membranes of isolated vacuoles of barley mesophyll cells. Images at low resolution indicate that vacuoles spontaneously attach, rupture and finally adsorb completely as planar membrane to mica. Height profiles indicate that the membrane at the peripheral boundary exposes the extravacuolar surface to the scanning tip. At molecular resolution a template matching correlation algorithm was used to identify the most abundant membrane protein, the vacuolar H+-ATPase by the characteristic extravacuolar head of the transport molecule. The data indicate the possibility to analyse single randomly distributed membrane proteins in their native environment with the knowledge of a suitable template.

M3 - Article

VL - 2001

SP - 100

EP - 107

JO - CONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES

JF - CONDENSED MATTER: STRUCTURAL, MECHANICAL, AND THERMAL PROPERTIES

IS - Vol.10(13)

ER -