Val arrow right Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein

Val arrow right Ala mutations within the effective transmembrane segment of a model single-spanning membrane, the 50-residue major coat (gene VIII) protein of bacteriophage M13, are shown to have sequence-dependent impact on stabilization of membrane-embedded helical dimeric structures. The overall...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-01, Vol.90 (24), p.11648-11652
Main Authors: Deber, C M, Khan, A R, Li, Zuomei, Joensson, C, Glibowicka, M, Wang, Jing
Format: Article
Language:English
Subjects:
phage M13
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Summary:Val arrow right Ala mutations within the effective transmembrane segment of a model single-spanning membrane, the 50-residue major coat (gene VIII) protein of bacteriophage M13, are shown to have sequence-dependent impact on stabilization of membrane-embedded helical dimeric structures. The overall results constitute an experimental approach to categorizing the distinctive contributions to structure of the residues comprising a protein-protein packing interface vs. those facing lipid and confirm the sequence-dependent capacity of specific residues within the transmembrane domain to modulate protein-protein interactions which underlie regulatory events in membrane proteins.
ISSN:0027-8424