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

The "microassembly" of integral membrane proteins: applications & implications.

J L Popot1, D M Engelman, G Zaccai

  • 1Institut de Biologie Physico-Chimique, Collège de France, Paris.

Progress in Clinical and Biological Research
|January 1, 1990
PubMed
Summary

Integral membrane proteins fold via a two-stage process where hydrophobic alpha-helices form independently before assembling. This model explains protein structure and biosynthesis in cellular membranes.

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

Surviving salt fluctuations: stress and recovery in Halobacterium salinarum, an extreme halophilic Archaeon.

Scientific reports·2020
Same author

Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.

Journal of the Royal Society, Interface·2015
Same author

Dynamics measured by neutron scattering correlates with the organization of bioenergetics complexes in natural membranes from hyperthermophile and mesophile bacteria.

The European physical journal. E, Soft matter·2013
Same author

Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteins.

Biophysical journal·2012
Same author

Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics.

Journal of the Royal Society, Interface·2012
Same author

Functional properties of the acetylcholine receptor protein.

Neurochemistry international·2010

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Integral membrane proteins are crucial for cellular functions.
  • Their transmembrane regions are often composed of hydrophobic alpha-helices.
  • Understanding their folding is key to understanding protein function.

Purpose of the Study:

  • To present evidence supporting a two-stage model for integral membrane protein folding.
  • To explore the role of autonomous folding domains (transmembrane alpha-helices).
  • To discuss the implications for biosynthesis and structural modeling.

Main Methods:

  • Analysis of known high-resolution integral membrane protein structures.
  • Experimental "microassembly" of functional proteins from folded fragments.

Related Experiment Videos

  • Examination of small integral subunits in organelle inner membranes.
  • Application of microassembly and neutron diffraction to bacteriorhodopsin.

    • Main Results:

    • Evidence supports a two-stage folding model: helix formation followed by packing.
    • Transmembrane helices can act as autonomous folding units.
    • Microassembly experiments confirm this folding pathway.
    • Small integral subunits suggest helix-based assembly.

    Conclusions:

    • The two-stage folding model provides a framework for understanding integral membrane protein structure.
    • This model has implications for protein biosynthesis and predicting structure from sequence.
    • Microassembly is a valuable tool for elucidating protein tertiary structures.