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Then, intermittent binding to a trap of a given radius.
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Tryptophan binding to TRAP shows only a small change in the Gibbs free energy of binding over a 25 50 °C range, with binding becoming gradually weaker as the temperature increases [ 21].
In the simplest model, spontaneous dissociation of DCC-SSB·dT70 would be followed by rapid binding to the trap.
This is interesting as Thr is known to be important for tryptophan binding to TRAP [ 39] and a hydrogen bond is found between tryptophan and the carbonyl oxygen of Thr in tryptophan-bound crystal structures.
Finally, intermittent binding to traps with a distribution of sizes.
The association rate for VEGF Trap binding to VEGF-A was orders of magnitude faster than that measured for bevacizumab and ranibizumab.
In previous calorimetry experiments, the ΔS of tryptophan binding to TRAP was found to be zero at approximately 287 K, becoming increasingly negative as the temperature was increased [ 21].
The photoinduced absorption transient measured at a wavelength of 1440 nm, corresponding to a trap binding energy of 40 meV, provides a trap state escape time of about 90 μs.
This can be explained by secondary recruitment of SG proteins via binding to RNA molecules trapped in the FAs by interaction with RNA-binding domains of FUS.
Interestingly, the catalytically inactive VopS mutation also enhances its binding to GTPase by a "substrate trap" [5].
Based on the hydrogen-binding to the traps in the bulk SiO2, a mechanism was proposed to explain the very short response time on the device with the ultra-thin SiO2.
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