Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



  history
ID: 318356.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Changes in the surface structure of purple membrane upon illumination measured by atomic force microscopy
Authors:Persike, N.; Pfeiffer, M.; Guckenberger, R.; Fritz, M.
Date of Publication (YYYY-MM-DD):2000
Title of Journal:Colloids and Surfaces B: Biointerfaces
Volume:19
Start Page:325
End Page:332
Audience:Not Specified
Abstract / Description:Bacteriorhodopsin (BR) patches with a diameter of 1 to 3 small mu, Greekm were investigated in their native state by atomic force microscopy (AFM) in buffer solution. The patches were immobilized deposited and investigated on mica in 150 mM KCl and 10 mM Tris-buffer at pH 8. Under this buffer condition they adsorb preferred with their extracellular side to the solid support mica. The structure of the two-dimensional light adapted crystals was resolved with an imaging force of about 100 pN up to a resolution of 13 Å. The topography of the surface gets smoother if an imaging force of 1000 pN was applied indicating that protruding structures are compressed. Upon illumination with white light, during imaging with a force of 200 pN, the surface structure of the BR lattice changed. The force- and light-induced structural changes were reversible.
Free Keywords:Bacteriorhodopsin; AFM-BIO
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.