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Chapter VII Reactivity at Dislocation….<br />

Log W<br />

-1.0<br />

-1.1<br />

-1.2<br />

-1.3<br />

-1.4<br />

-1.5<br />

-1.6<br />

0.00320 0.00324 0.00328 0.00332 0.00336<br />

1/T<br />

270<br />

Pure KDP<br />

KDP + 0.3 Wt. % L-threonine<br />

KDP + 0.4 Wt. % L-threonine<br />

KDP + 0.5 Wt. % L-threonine<br />

Figure:7.5 Plots of log W 1/T for pure and L-threonine doped KDP crystal.<br />

Log W<br />

-1.0<br />

-1.1<br />

-1.2<br />

-1.3<br />

-1.4<br />

-1.5<br />

-1.6<br />

0.00320 0.00324 0.00328 0.00332 0.00336<br />

1/T<br />

Pure KDP<br />

KDP + 0.3 Wt. % DL-methionine<br />

KDP + 0.4 Wt. % DL-methionine<br />

KDP + 0.5 Wt. % DL-methionine<br />

Figure :7.6 Plots of log W 1/T for pure and DL-methionine doped KDP crystal.<br />

From table 7.1, one can observe that the activation energy is highest for pure<br />

KDP crystals compared to amino acids doped KDP crystals. Further, the<br />

activation energy slowly decreases from L-histidine to L-threonine and then to<br />

DL-methionine. The lower values of activation energy for amino acids doped

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