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Figure 1.

Schematic diagram of FRET assay for evaluating the cleavage efficiency of restriction endonucleases.

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Table 1.

Oligonucleotides used in this study.

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Figure 2.

Effects of enzyme concentrations on EcoRV cleavage.

(A) Time course plot of fluorescence intensity. (B) Initial velocities affected by enzyme concentrations.

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Figure 3.

Effects of 2′-OMeN and PS substitution positions on EcoRV cleavage.

(A) Time course plot of fluorescence intensity of 2′-OMeN substitution. (B) Initial velocities affected by position-dependent 2′-OMeN substitution. (C) Time course plot of fluorescence intensity of PS substitution. (D) Initial velocities affected by position-dependent PS substitution.

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Figure 3 Expand

Figure 4.

Relative initial velocities (RV) of SpeI cleavage affected by position-dependent substitution.

(A) Effects of 2′-OMeN substitution positions. (B) Effects of PS substitution positions.

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Figure 4 Expand

Figure 5.

Relative initial velocities (RV) of XbaI cleavage affected by position-dependent substitution.

(A) Effects of 2′-OMeN substitution positions. (B) Effects of PS substitution positions.

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Figure 5 Expand

Figure 6.

Relative initial velocities (RV) of XhoI cleavage affected by position-dependent substitution.

(A) Effects of 2′-OMeN substitution positions. (B) Effects of PS substitution positions.

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Figure 6 Expand

Figure 7.

Relative initial velocities (RV) of PstI cleavage affected by position-dependent substitution.

(A) Effects of 2′-OMeN substitution positions. (B) Effects of PS substitution positions.

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Figure 7 Expand

Figure 8.

Relative initial velocities (RV) of SphI cleavage affected by position-dependent substitution.

(A) Effects of 2′-OMeN substitution positions. (B) Effects of PS substitution positions.

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Figure 8 Expand

Table 2.

Relative initial cleavage rate of 2′-OMeN modification.

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Table 2 Expand

Table 3.

Relative initial cleavage rate of PS modification.

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Table 3 Expand