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Membrane protein folding: beyond the two stage model
Author(s) -
Engelman Donald M.,
Chen Yang,
Chin Chen-Ni,
Curran A.Rachael,
Dixon Ann M.,
Dupuy Allison D.,
Lee Albert S.,
Lehnert Ursula,
Matthews Erin E.,
Reshetnyak Yana K.,
Senes Alessandro,
Popot Jean-Luc
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01106-2
Subject(s) - folding (dsp implementation) , protein folding , biophysics , chemistry , membrane , protein quaternary structure , membrane protein , protein structure , crystallography , biology , biochemistry , engineering , protein subunit , electrical engineering , gene
The folding of α‐helical membrane proteins has previously been described using the two stage model, in which the membrane insertion of independently stable α‐helices is followed by their mutual interactions within the membrane to give higher order folding and oligomerization. Given recent advances in our understanding of membrane protein structure it has become apparent that in some cases the model may not fully represent the folding process. Here we present a three stage model which gives considerations to ligand binding, folding of extramembranous loops, insertion of peripheral domains and the formation of quaternary structure.