a Journal of Postdoctoral Research and Postdoctoral Affairs.
    ISSN : 2328-9791
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The molecular structure and the folding of the whole Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): corrector sites
Author(s) : Satriano L, Cossu C, Baroni D, Zegarra-Moran O, Ford F, Pollock N, Moran O
Address : Istituto di Biofisica, CNR, Genova, Italy, Unit√† Operativa di Genetica Medica, Istituto G. Gaslini, Genova, Italy, Faculty of Life Sciences, University of Manchester, Manchester, UK 
Multiple Institutions in collaboration

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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