期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 70, 期 4, 页码 1488-1497出版社
WILEY
DOI: 10.1002/prot.21642
关键词
Vpu; HIV-1; membrane proteins; artificial bilayers; ion channels; gating
Vpu from HIV-1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu(1-32)) and mutant peptides (Vpu(1-32) W23L, Vpu(1-32)-R31V, Vpu(1-32)-d S24L) have been synthesize and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu(1-32)-W23L has a considerable flickering pattern in the recordings and longer open times than Vpu(1-32)-Whilst recordings for Vpu(1-32)-R31V are almost indistinguishable from those of the WT peptides re-S24L do not exhibit any noticeable channel activity. Recording of WT peptide and Vpu(1-32)-32-W23L indicate Michaelis-Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics.
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