Abstract
The difficulties encountered in the crystallization of membrane proteins in a form suitable for X-ray analysis have stimulated the development of algorithms to predict, from primary amino acid sequences, the locations of transmembrane spans based upon assessment of local hydrophobicity. The proposed models for the folding of polypeptide chains of a variety of integral proteins predict membrane-spanning α-helices connected by hydrophilic, looplike segments. To test the validity of such models, much interest has been devoted to various probes that are important tools in studying the spatial orientation of membrane-spanning polypeptide chains (for review see Ovchinnikov, 1987).
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© 1989 Springer-Verlag Berlin Heidelberg
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Brandolin, G., Boulay, F., Dalbon, P., Block, M., Gauche, I., Vignais, P.V. (1989). Immunological and Enzymatic Approaches of the Orientation of the Membrane Bound ADP/ATP Carrier. In: Azzi, A., Nałęz, K.A., Nałęcz, M.J., Wojtczak, L. (eds) Anion Carriers of Mitochondrial Membranes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74539-3_12
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DOI: https://doi.org/10.1007/978-3-642-74539-3_12
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