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We find that the binding of the proteins to the ice surfaces is irreversible ("Superheating of ice crystals in antifreeze protein solutions" PNAS 2010 and "Microfluidic experiments reveal that antifreeze proteins bound to ice crystals suffice to prevent their growth" PNAS 2013).
These effects on the branchpoint sequence may reflect non-specific binding of the proteins.
The binding of the proteins to PLG was also evaluated by ELISA.
PCR assays were performed to assess the binding of the proteins to the pS2 5' flanking sequence.
These four repeats form the conserved core region, which is responsible for the Ca2+-dependent binding of the proteins to phospholipids [56].
As depicted in Fig. 4A, when 2 mM ACA was added to the reaction, the binding of the proteins to PLG was almost completely abolished.
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Consequently, the question whether binding of the protein is adsorptive or covalent is still unanswered.
The area of MPA was locally activated to reactive esters to permit the binding of the protein.
The heat capacity increments associated with the binding of the protein ligands and contact interaction between the bound ligands were comparable by value but opposite in sign.
A strong NADH binding in contrast to weaker NAD+ binding of the protein was inferred from fluorometrically determined binding constants for the dinucleotide cofactor.
The hydrophobic moieties of DT functions allow the proteins to approach the activated receptor more easily, resulting in the binding of the protein to the activated MPA sites via carboimide coupling to protein-free anime moieties.
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