Abstract:
:We have studied the effects of 'hydrophobic mismatch' between a poly-Leu transmembrane helix (TMH) and the ER membrane using a glycosylation mapping approach. The simplest interpretation of our results is that the lumenal end of the TMH is located deeper in the membrane for both short (negative mismatch) and long (positive mismatch) TMHs than for poly-Leu segments of intermediate length. We further find that the position-specific effect of Lys residues on the location of short TMHs in the membrane varies with an apparent helical periodicity when the Lys residue is moved along the poly-Leu stretch. We discuss these findings in the context of models for peptide-lipid interactions during hydrophobic mismatch.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Monné M,von Heijne Gdoi
10.1016/s0014-5793(01)02415-2keywords:
subject
Has Abstractpub_date
2001-05-11 00:00:00pages
96-100issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02415-2journal_volume
496pub_type
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