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First, relative to WT PA, the M662R mutant may form two extra salt bridges with TEM8 (Figure 5B): one with Tyr119 (Tyr119 in CMG2) and the other with Asp117 (Glu117 in CMG2).
In particular, a slowly growing mutant may form more biofilm than a fast-growing mutant.
This may be a consequence of prc1-1 having a reduced epidermal cell length or alternatively the mutant may form more root hairs compared to wild-type.
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The simplest conclusion from these experiments, however, is that neither mfold 1 nor mfold 2 represent the sole active confirmation, although it is possible that these mutants may form another structure that can present the TURBS motif 1 to helix 26 of 18S rRNA.
As may be inferred from protein docking experiments, the R70Q mutant tetramers may form an extra hydrogen bond with R54 of IRAK-4 tetramers, but loose the R70 interaction points with IRAK-2.
Alternatively, newly synthesized mutant SOD1 proteins may form amyloid before metals are coordinated.
Since formin family proteins are known to function as a dimer (Goode and Eck, 2007; Pollard, 2007), such a mutant Fhod3 protein may form a non-functional heterodimer with the wild-type protein, raising the possibility that a loss-of-function mutation in the FHOD3 gene may cause familial cardiomyopathy with autosomal dominant inheritance.
Because CAPS-associated mutant NLRP3 is not protected by CARD8, it may form inflammasome without obvious stimulation.
Divisive rival camps may form.
A few females may form spinster herds.
Sometimes, wetlands may form.
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