Sequence alignments of IC3-C58 with S100B binding sequences from p53, NDR kinase, and TRTK-12 showed there are no clear sequence similarities in any of these peptides other than a basic pI and several hydrophobic residues in the sequences.
Multiple copies of ITS2 were recovered in eight strains (from groups A, B, D, F and G; Additional file 2), i.e. there were no clear sequence reads possible without cloning.
Interestingly RLIP76/RalBP1, a protein with Cdc42 GAP activity, interacts with the ENTH domain of epsin (Rossé et al., 2003), although there is no clear sequence homology between RLIP76/RalBP1 and Rga proteins.
Amino acid frequency analysis of the acetylated residues of these over 200 "internal" acetylated N-termini showed that there was no clear consensus sequence, in sharp contrast to proteins that are acetylated at position 1 or 2, i.e. specifically by the N-acetyltransferase complexes NatA or NatB.
There was no clear difference in sequence classes between XLMR and non-XLMR.
Similarly, there was no clear indication that any particular sequence of agents is preferable.
Potential novel miRNAs were discarded from the final collection when they were reported as deriving from heterogeneous precursor positions or there was no clear dominance of their specific sequence from one arm of the proposed hairpin structure.
In contrast to the previously designed Adap, the base-pairing and fluorescence quenching properties of 2-amino-Adap varied depending on the ODN sequence, and there was no clear indication of an additional hydrogen bond with 8-oxo-dG.
However, there was no clear separation into sub-groups of orthologous sequences within the dicots group.
By contrast, there was no clear correlation between the density of Alu sequences and CBPs (see Additional file 6, Figure S3A).
