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Adding hydroxyl groups slowed diffusion of hydronium ions within a cluster due to tighter binding in the interface and enhanced diffusion between clusters due to better connectivity.
Electron transfer is enabled by calmodulin binding in the interface between the two domains.
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Probably, the high energy cost of this process may be decreased via local perturbations of the membrane in response to the initial toxin binding in the interface-inserted mode.
Structural modelling predicts that the interface mutation prevents the intersubunit linker from binding in the dimer interface, allowing the active sites to form in the procaspase in the absence of cleavage.
We then identified the binding segments in the interface of the query complex.
The observed time-dependent variations in contractile parameters may occur due to biological changes inherent to neoCMs in culture or variations in time of laminin binding stability in the interface between PDMS surfaces and neoCMs.
Upon cleavage of the IL (intersubunit linker) by initiator caspases, the polypeptide chain is released from its binding in the dimer interface cavity, allowing the substrate-binding loop (called L3) to move into the active site and form the base of the substrate-binding pocket [ 5].
No hot spots for binding were found in the interface, with individual mutations having an up to fivefold effect on binding.
Many of the residues involved in binding at the interface between monomers are well conserved, with notable differences highlighted by the position of red spheres in Figure 11A.
Mutational studies revealed a pocket of amino acids outside the orthosteric substrate binding sites located in the interface between extracellular loops 1 and 3 that when mutated affect transporter function.
This latter folding upon binding event results in the interface shown in Figure 8.
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