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The Stern Volmer quenching constant (KSV) and corresponding thermodynamic parameters (ΔG, ΔH and ΔS) of the binding processes were determined.
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With the simultaneous use of SGTP and GTP affinity probes, 165 proteins involved in different biological processes were determined to be SGTP-binding targets.
In experimental as well as predicted p[STY]-protein sets, proteins with function in "translation", "RNA binding", "biosynthetic process" were determined as underrepresented.
The binding strength and the number of binding sites were determined at different ionic strengths.
The binding parameters were determined by fluorescence anisotropy measurements.
In vitro GRPR-binding affinities were determined with competitive binding assays on PC3 human prostate cancer cells.
Molecular dynamics based free energy calculations of the peptide binding process are used to determine the interactions as well as the important amino acid residues involving in binding.
Stability, protein binding and logP values were determined.
It was found that the core templates rather than functional groups play a larger role during the binding processes; in addition, the binding qualities are determined by the synergistic effects of the core templates and functional groups.
The binding constant and binding site size between the two species were determined to be 3.7 × 105 L mol−1 and 4.2, respectively.
The binding specificity of bead binding was determined following protocols described previously [8].
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