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As the beads were not continuously agitated upon irradiation with light, several of the beads are colored on only one half
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As the beads were not continuously agitated upon irradiation with light, several of the beads are colored on only one half.
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47
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0029811207
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In control experiments with a tripeptide library of the general structure Ac-AA3-AA2-AA1-resin with no linkers between the amino acids, AgNP formation was not observed under identical conditions. This experiment further supports the importance of the rigid linker. For the importance of turn-inducing linkers in peptide binding to metal ions other than Ag+, see: M. B. Francis, N. S. Finney, E. N. Jacobsen, J. Am. Chem. Soc. 1996, 118, 8983-8984.
-
In control experiments with a tripeptide library of the general structure Ac-AA3-AA2-AA1-resin with no linkers between the amino acids, AgNP formation was not observed under identical conditions. This experiment further supports the importance of the rigid linker. For the importance of turn-inducing linkers in peptide binding to metal ions other than Ag+, see: M. B. Francis, N. S. Finney, E. N. Jacobsen, J. Am. Chem. Soc. 1996, 118, 8983-8984.
-
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48
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70349947039
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All possible diastereoisomers of peptides 2 a and 3 a were examined and showed essentially the same results, which demonstrates that the absolute configuration of the amino acids is of minor importance for activity
-
All possible diastereoisomers of peptides 2 a and 3 a were examined and showed essentially the same results, which demonstrates that the absolute configuration of the amino acids is of minor importance for activity.
-
-
-
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49
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70349954740
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-
Negative control experiments with peptides that were not hits in the combinatorial assay (e.g, Ac-Tyr-Gly-Tyr-TG) did not form AgNPs under identical conditions
-
Negative control experiments with peptides that were not hits in the combinatorial assay (e.g., Ac-Tyr-Gly-Tyr-TG) did not form AgNPs under identical conditions.
-
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-
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50
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