tetano
Editor, Senior Moderator
Angew Chem Int Ed Engl. 2001 Jan 19;40(2):369-373. doi: 10.1002/1521-3773(20010119)40:2<369::AID-ANIE369>3.0.CO;2-7.
[h=1]Synthesis and Membrane-Binding Properties of a Characteristic Lipopeptide from the Membrane-Anchoring Domain of Influenza Virus A Hemagglutinin.[/h] Eisele F[SUP]1[/SUP], Kuhlmann J[SUP]2[/SUP], Waldmann H[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] On the trail of the influenza virus! Fluorescent-labeled lipopeptides, such as the characteristic S-palmitoylated partial structure from influenza virus hemagglutinin A, can be synthesized efficiently by employing a new enzymatic protecting-group technique in the key steps. Their binding to model membranes was determined in a kinetic assay, so leading to a first approximation of the membrane-anchoring ability of the corresponding lipopeptide motif in the parent protein.
[h=4]KEYWORDS:[/h] enzyme catalysis; fluorescence; membranes; peptides; protecting groups
PMID: 29712417 DOI: 10.1002/1521-3773(20010119)40:2<369::AID-ANIE369>3.0.CO;2-7
[h=1]Synthesis and Membrane-Binding Properties of a Characteristic Lipopeptide from the Membrane-Anchoring Domain of Influenza Virus A Hemagglutinin.[/h] Eisele F[SUP]1[/SUP], Kuhlmann J[SUP]2[/SUP], Waldmann H[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] On the trail of the influenza virus! Fluorescent-labeled lipopeptides, such as the characteristic S-palmitoylated partial structure from influenza virus hemagglutinin A, can be synthesized efficiently by employing a new enzymatic protecting-group technique in the key steps. Their binding to model membranes was determined in a kinetic assay, so leading to a first approximation of the membrane-anchoring ability of the corresponding lipopeptide motif in the parent protein.
[h=4]KEYWORDS:[/h] enzyme catalysis; fluorescence; membranes; peptides; protecting groups
PMID: 29712417 DOI: 10.1002/1521-3773(20010119)40:2<369::AID-ANIE369>3.0.CO;2-7