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Receptor-ligand interactions between synthetic peptides and normal human erythrocytes were studied to determine P. falciparum merozoite surface protein-10 (MSP-10) regions specifically binding to membrane surface receptors on human erythrocytes.
This early paper details the critical fact that protein binding to membrane surface modulates miscibility phase transitions.
All B. thuringiensis crystal proteins (Cry proteins) which are toxic to target insects share general traits in their mode of action: solubilization in the midgut, activation by gut proteases, binding to membrane surface proteins (generally referred to as 'receptors') [ 6, 7].
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Permanent binding of tissue factor F3 to membrane surface is thought to be crucial for the speed of enzymatic reactions in coagulation processes [ 67].
However, growing evidence indicates that steroid hormones also exert rapid cell surface-initiated actions by binding to membrane receptors [ 39], such as the estrogen membrane receptor GPR30 [ 14].
The exponential model fitting calculations shows that increasing Eu3+ concentrations significantly affected the binding of Aβ42 to membrane surfaces, and that Eu3+ caused an increase in the time taken for Aβ42 to initially associate with LUVs. 10 μM Eu3+ caused a 5.4 fold delay in the initial association and formation of defects in the membrane compared to when Eu3+ was absent (Table 3, t1 and t2).
Comparison with published free energy scales indicates that the reduced electrostatic contribution to binding to membranes having reduced negative surface charge can be compensated in RTA3 (but not RTA3-C15S) by a slightly deeper insertion of the C-terminus of the peptide to maximize hydrophobic contributions to binding.
Peptide-induced membrane permeabilization follows binding to the membrane surface.
"Hybrid" proteins, such as N-BAR domains, with both insertion and scaffolding effects, are predicted to generate coexisting vesicles and tubules with the degree of preference for the former or latter depending on the amount of the amphipathic helices per scaffold and on the effective rigidity of the scaffold, which includes the strength of the scaffold binding to the membrane surface.
Examples include membrane-curvature control of dynamin polymerization 104, phosphocholine cytidylyltransferase activity 105, and the binding of bar domains to membrane surfaces 22, 23, 106, 107 as illustrated in Fig. 10.
One vehicle driving the intracellular signal transduction speed beyond that of simple diffusion is the selective and reversible binding of so-called peripheral proteins to membrane surfaces within the cell (Hurley, 2006; Pawson and Scott, 1997).
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