作者: Joseph Strzalka , Xiaoxi Chen , Christopher C. Moser , P. Leslie Dutton , Benjamin M. Ocko
DOI: 10.1021/LA000264Z
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摘要: We present isotherm and X-ray reflectivity (XR) measurements from Langmuir monolayers of a de novo synthetic di-α-helical peptide, consisting two identical 31-residue, mostly α-helical peptide units joined by disulfide bond at their amino-termini. Fitting the XR data to slab models shows that dihelices lie in plane interface low pressures. The were insufficiently stable for study high pressures, but films based on derivative alkylated its amino termini permitted investigations over larger range observed an orientational transition, which α-helices begin lying surface pressures orient themselves approximately normal draw same conclusions when we analyze it using box refinement, iterative, model-independent method recovering structure data. Mixtures these palmitoylated peptides with fatty acid (...