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Biophysical and computational studies of membrane penetration by the GRP1 pleckstrin homology domain.

Abstract:

The pleckstrin homology (PH) domain of the general receptor for phosphoinositides 1 (GRP1) exhibits specific, high-affinity, reversible binding to phosphatidylinositol (3,4,5)-trisphosphate (PI(3,4,5)P(3)) at the plasma membrane, but the nature and extent of the interaction between this bound complex and the surrounding membrane environment remains unclear. Combining equilibrium and nonequilibrium molecular dynamics (MD) simulations, NMR spectroscopy, and monolayer penetration experiments, we...

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Publication status:
Published

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Publisher copy:
10.1016/j.str.2011.04.010

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Journal:
Structure (London, England : 1993) More from this journal
Volume:
19
Issue:
9
Pages:
1338-1346
Publication date:
2011-09-01
DOI:
EISSN:
1878-4186
ISSN:
0969-2126

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