Sequence and length optimization of membrane active coiled coils for triggered liposome release
نویسندگان
چکیده
منابع مشابه
Length-dependent force characteristics of coiled coils.
Coiled-coil domains within and between proteins play important structural roles in biology. They consist of two or more alpha helices that form a superhelical structure due to packing of the hydrophobic residues that pattern each helix. A recent continuum model showed that the correspondence between the chirality of the pack to that of the underlying hydrophobic pattern comes about because of t...
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Most recently, X-ray crystallography of a soluble synaptic fusion complex formed between two helical segments of SNAP-25 and the C-terminal regions of synaptoJohn J. Skehel* and Don C. Wiley†‡ *National Institute for Medical Research The Ridgeway Mill Hill brevin and syntaxin, expressed without their membrane London, NW7 1AA, England United Kingdom †Department of Molecular and Cellular Biology ...
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We introduce Paircoil2, a new version of the Paircoil program, which uses pairwise residue probabilities to detect coiled-coil motifs in protein sequence data. Paircoil2 achieves 98% sensitivity and 97% specificity on known coiled coils in leave-family-out cross-validation. It also shows superior performance compared with published methods in tests on proteins of known structure.
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The stability and compatibility of designed coiled coil peptides towards the selective incorporation of γ(4)-amino acids at the hydrophobic positions of the heptad repeat are studied. Investigations reveal that the low thermal denaturation temperature of γ(4)-residue mutated coiled coils can be utilized as a mild hyperthermia trigger in liposomes.
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2019
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2018.11.005