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Membrane protein folding and oligomerization: the two-stage model

Popot, J. L., Engelman, D. M.·1990·Biochemistry

Abstract

We discuss the view that the folding of many, perhaps most, integral membrane proteins can be considered as a two-stage process. In stage I, hydrophobic alpha-helices are established across the lipid bilayer. In stage II, they interact to form functional transmembrane structures. This model is suggested by the nature of transmembrane segments in known structures, refolding experiments, the assembly of integral membrane protein from fragments, and the existence of very small integral membrane protein subunits. It may extend to proteins with a variety of functions, including the formation of transmembrane aqueous channels. The model is discussed in the context of the forces involved in membrane protein folding and the interpretation of sequence data.

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Metadata

Authors
Popot, J. L., & Engelman, D. M.
Venue
Biochemistry
Published
1990-05-01
Volume
29
Issue
17
Pages
4031-4037
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2027711565
Cited by
932
References
0
FWCI
7.43
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Membrane protein folding and oligomerization: the two-stage model. https://app.cochat.ai/papers/10.1021/bi00469a001
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Popot, J. L., & Engelman, D. M. (1990). Membrane protein folding and oligomerization: the two-stage model. Biochemistry. https://doi.org/10.1021/bi00469a001

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.