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The molecular structure and the folding of the whole Cystic Fibrosis Transmembrane Conduc
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Author(s) : Satriano L, Cossu C, Baroni D, Zegarra-Moran O, Ford F, Pollock N, Moran O
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Address : Istituto di Biofisica, CNR, Genova, Italy, Unità Operativa di Genetica Medica, Istituto G. Gaslini, Genova, Italy, Faculty of Life Sciences, University of Manchester, Manchester, UK
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Multiple Institutions in collaboration
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Info@Postdocjournal.Com
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Background and rationale. CFTR is an anionic channel expressed in epithelia whose mutations cause cystic fibrosis, but its structure is still unknown.
Hypothesis and objectives. We explored a set of structural parameters of the wild type and mutated (F508del) CFTR by physical methods.
Essential methods. WT and F508del CFTR were over-expressed in yeast, solubilised in the detergent LPG-14 and purified. The detergent-CFTR complexes were studied by SAXS techniques using a solvent of variable density.
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