Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structural determinants of purple membrane assembly.

M P Krebs1, T A Isenbarger

  • 1Department of Biomolecular Chemistry, University of Wisconsin Medical School, 53706-1532, Madison, WI, USA. mpkrebs@facstaff.wisc.edu

Biochimica Et Biophysica Acta
|September 14, 2000
PubMed
Summary

Bacteriorhodopsin assembly in purple membranes is driven by protein-lipid interactions, with some contribution from protein-protein contacts. Understanding these forces offers insights into membrane protein complex formation.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Disruption in murine Eml1 perturbs retinal lamination during early development.

Scientific reports·2020
Same author

Genomic perspective on the photobiology of Halobacterium species NRC-1, a phototrophic, phototactic, and UV-tolerant haloarchaeon.

Photosynthesis research·2005
Same author

The cobY gene of the archaeon Halobacterium sp. strain NRC-1 is required for de novo cobamide synthesis.

Journal of bacteriology·2002
Same author

Thermodynamic stability of the bacteriorhodopsin lattice as measured by lipid dilution.

Biochemistry·2001
Same author

An improved tripod amphiphile for membrane protein solubilization.

Protein science : a publication of the Protein Society·2001
Same author

brp and blh are required for synthesis of the retinal cofactor of bacteriorhodopsin in Halobacterium salinarum.

The Journal of biological chemistry·2000

Area of Science:

  • Structural biology
  • Biophysics
  • Membrane protein biochemistry

Background:

  • Purple membrane from Halobacterium salinarum serves as a model system for integral membrane protein complex assembly.
  • High-resolution structures and lipid composition data facilitate studies on assembly forces.
  • Bacteriorhodopsin is a key protein component of the purple membrane.

Purpose of the Study:

  • To review recent mutational studies on bacteriorhodopsin.
  • To identify structural features governing purple membrane assembly.
  • To elucidate the driving forces behind integral membrane protein complex formation.

Main Methods:

  • Mutational analysis of bacteriorhodopsin.
  • Structural studies.
  • Calorimetric studies.

Related Experiment Videos

  • Reconstitution studies.

    • Main Results:

    • Interactions between transmembrane helices of neighboring bacteriorhodopsin molecules contribute to assembly.
    • Specific protein-lipid interactions appear to be the major driving force for purple membrane assembly.
    • Mutational efforts identified key structural features influencing bacteriorhodopsin assembly.

    Conclusions:

    • Protein-lipid interactions are crucial for purple membrane assembly.
    • Understanding these interactions provides insights into broader principles of membrane protein complex formation.
    • Further research into protein-protein and protein-lipid interactions is warranted.