The secondary and tertiary structure of this sequence exhibited structural similarity to TIR domain family.
Consistent with the previous results25, the fusion protein with the wild-type (WT) mifM sequence exhibited very low β-galactosidase activity (0.6 Miller units; Fig. 1B).
The subject's DNA sequence exhibited only the reference allele at 99.4% of the markers homozygous for the reference and at 95.1% of markers homozygous for the variant.
The probe with 4egg attenuating sequence exhibited the highest CPP/attenuator interaction, predicting minimized cellular uptake until cleaved.
The Atlantic salmon sequence exhibited highest amino acid identity to rainbow trout TR-α (98%), Japanese flounder TR-αB (93%), and zebrafish TR-α1 (90%).
Introduction of Glu217 into trypsin variants containing the SSFI sequence exhibited enhanced affinity for the factor Xa ligands (2) and (3).
Upon translation of the cDNA, FcEP-1 was predicted to consist of 648 amino acids, and the protein sequence exhibited similarity to vertebrate and invertebrate vitellogenins.
In vitro the single-strand recombinant phagemid vector containing the combination sequence exhibited 10 23 deoxyribozyme activity, and the linear transcript displayed hammerhead ribozyme activity.
The in silico predicted feline HCA2 protein sequence exhibited 83.1% and 86.5% amino acid similarity to human and mouse sequences, respectively.
The non-complementary sequence exhibited negligible signal change compared with the blank measurement (means: the electrode containing no target DNA incubating in hybridization buffer solution containing Cu-DNCs DNA probe for a certain time).
Polyclonal antibodies raised against the HB-peptide sequence, exhibited high binding specificity and sensitivity to the HB-fused recombinant proteins (∼10 ng) in different crude cell extracts obtained from diverse expression hosts.
