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Binding of the α1E2 peptide to these DNA sequences display a different counter-ion dependence, indicating a dissimilar, sequence-dependent mechanism of interaction.
Tropoelastin and elastin-derived polypeptide sequences display a thermally reversible phase transition above a lower critical solution temperature, Tt, which coincides with the development of elastomeric restoring force in the material.
Interestingly, the curves for the codirectional overlapping sequences display a crossing at length ~75 base pairs.
The signal peptide sequences display a strong conservation in the amino acid sequence.
In contrast, chicken and other studied teleost Nme4 sequences display a hydrophilic residue in position 90.
These two sequences display a low level of sequence identity (less than 30%), especially concentrated in the C-terminal segment.
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We further amplified and sequenced position 297 on exon 6. Twelve sequences display an A at position 297, which is compatible with the most frequent O haplotype, the O01, but not with the other, the O02 [ 5].
Two of three internal peptide sequences displayed a significant similarity to the family of fibrinogen-related molecules.
Lastly, viral talC sequences displayed a high occurrence of same-scaffold viral neighbors (67%).
One of these sequences displayed a recombination breakpoint in the gp120 C2 region.
Multiple sequence alignments of SCRiP sequences displayed a high degree of diversity except for the conserved cysteine sites.
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