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Helical membrane protein folding, stability, and evolution.

J L Popot1, D M Engelman

  • 1Laboratoire de Physicochimie Moléculaire des Membranes Biologiques, Centre National de la Recherche Scientifique UPR 9052, Institut de Biologie Physico-Chimique, F-75005 Paris, France. jean-luc.popot@ibpc.fr

Annual Review of Biochemistry
|August 31, 2000
PubMed
Summary

Membrane protein folding involves two stages: helix formation and their association. This two-stage model aids in understanding stability, folding, and evolution of these crucial biological molecules.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Membrane proteins are essential for cellular functions.
  • Their folding and oligomerization are complex processes.
  • Understanding these processes is key to deciphering protein function and disease.

Purpose of the Study:

  • To present a conceptual framework for understanding helical membrane protein folding and oligomerization.
  • To analyze the interactions governing these processes.
  • To highlight the utility of a two-stage model.

Main Methods:

  • Conceptual analysis of existing evidence.
  • Examination of helix-bilayer interactions.
  • Review of helix-helix association mechanisms.

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Main Results:

  • Helical membrane protein folding and oligomerization can be viewed as two distinct energetic stages.
  • Stage 1: Formation of independently stable transbilayer helices.
  • Stage 2: Side-to-side association of these helices.

Conclusions:

  • The two-stage model simplifies discussions of membrane protein stability.
  • It provides a useful framework for membrane protein folding concepts.
  • It serves as a basis for understanding membrane protein evolution.