Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif |
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Authors: | Orzáez Mar Lukovic Dunja Abad Concepción Pérez-Payá Enrique Mingarro Ismael |
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Institution: | Departament de Bioquímica i Biologia Molecular, Universitat de València, E-46100 Burjassot, Spain. |
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Abstract: | The principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix-helix association and/or dissociation between TM fragments. |
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Keywords: | GpA Glycophorin A SDeS sodium decyl sulfate SDS-PAGE sodium dodecyl sulfate polyacryamide-gel electrophoresis STS sodium tetradecyl sulfate TM transmembrane |
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