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A study of the thermodynamic properties of the variants shows that the structure of UCH-L1 is remarkably tolerant to incorporation of bulky tryptophan side chains.
A comparative study of the reactivity of each plasma with respect to each of the variants shows that the response to both variants was strongly correlated (Pearson's test r = 0.8, p<.0001; Figure 6D), confirming that the VAR2CSA domaindomain contained conserved epitopes.
Comparison between the human neuroligins and the AmNLG3 variants shows that the first alternative splice site (A) of the human neuroligins is conserved in AmNLG3 (Figure S3) and the second splice site (B) in human NLG1 maps precisely to the intron/exon 3 4 splice junction in AmNLG3.
Comparison of the rates from the wild-type and V96P/N142M variants shows that the V96P/N142M membranes exhibit ~80% of the wild-type activity (see Supplementary Table S3 at http://www.biochemj.org/bj/456/bj4560139add.htm).htm
Their model, in addition to several variants, shows that class transitions can reduce top-down control of prey and stabilize dynamics by moving predator-prey cycles to point attractors.
Overall, the expression pattern of GRP splice variants shows that the GRP-F1, coding for the full protein, is the main transcript present in control skin and mammary gland.
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Phylogenetic analyses of the amino acid sequences of CYP102A1 variants showed that three variants are closely related to CYP102A1.1 and five variants are distinct from it (Figure 1a).
Truncated variants showed that EBR28 interacted with the catalytic domain of IN interfering with the binding of the DNA substrate.
Comparison of the variants showed that the use of multiple teflon foam interlayers could drastically reduce the average stress in the multilayer material.
Sequence data obtained from these variants showed that PCR-RFLP pattern differences reflected actual changes in predicted amino acid composition and that minor amino acid changes in a 23 base pair "NINNIY" repeat region (a conserved UspA1 and UspA2 binding site for the neutralising antibody mAb17C7) occurred.
At one level the network behaves as a rigid unit that does not readily reorganize when disrupted: crystal structures of the E75A or E75Q variants show that even when the pivotal Glu75 is removed, the overall configuration of the network was unaffected.
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