Sentence examples for is predicted to repeat from inspiring English sources

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Carl Edwards, above, is predicted to repeat last year's victory.

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The N-terminus is predicted to contain armadillo (ARM) repeats and ankyrin repeats, followed by a leucine-rich repeat (LRR) domain, a Ras of complex (Roc) GTPase domain, a C-terminal of Roc (COR) domain, a tyrosine kinase domain with greatest sequence similarity to the mixed-lineage kinase subclass of mitogen-activated protein kinase kinase kinases (MAPKKKs), followed by a C-terminal WD40 domain.

While the stability of both CCCCGG and GGGGCC repeat transcripts increases with increasing repeat length, the CCCCGG repeat is predicted to be less stable than its GGGGCC counterpart, which may decrease its susceptibility to RAN translation.

TBCD (pink, top panel) is predicted to consist of HEAT repeats.

Scc3 is predicted to be a HEAT repeat-containing protein and interacts with Scc1 to further strengthen the ring structure of cohesin.

This gene is predicted to encode a transducin/WD40 repeat-like superfamily protein with a DWD motif, which is involved in protein complex formation.

miR158 was described as a non-conserved miRNA from Arabidopsis that could, for example, not be detected in citrus [ 27]. miR158 is predicted to target a pentatricopeptide repeat-containing protein of unknown function, a lipase, and xyloglucan-fucosyl transferases [ 28].

Whether the repeat sequence is a pure CAG or an interrupted CAG is predicted to influence somatic instability of the repeat, with a pure repeat being far more unstable and tending to expand [19], [55] [57].

BamD is predicted to be rich in tetratricopeptide repeat (TPR) structure [25], a feature it shares with the mitochondrial receptor for β-barrel proteins [23], [27].

LM5578_1866 is predicted to encode a Sel1-like repeat (SLR) family protein that contains helical domains mediating protein-protein interactions [ 55].

The peptide encoded by each mmr-b repeat is predicted to form a series of alpha helices, with each helix composed of a hydrophobic side dominated by aliphatic residues that would be buried within the globular protein, and a polar side exposed to the extracellular environment [ 25, 27].

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