Derivatization on substituted phenyl groups at the 5- and 7-positions of 2 revealed that a 3,4-methylenedioxyphenyl group at the 5-position and a 4-methoxyphenyl group at the 7-position were optimal for binding affinity.
Highly sulfated forms can fail to support adhesion, whereas low-sulfated forms are optimal for binding [69], [70] and appear on the syncytiotrophoblast and in intervillous spaces [70].
The T and C in this position are optimal for binding the B-ZIP proteins CREB and C/EBP, respectively (Johnson 1993).
Molecular changes were made at the PAT C(4 -position, while preserving N,N-dimethyl substitution at the 2-position as well as trans-stereochemistry, structural features previously shown to be optimal for 5-HT2 binding.
The context information provided by the ten neighbouring residues was found to be optimal for DNA-binding site prediction [ 9, 10].
We believe that a bandwidth of 100 to 400 bp may be optimal for most TF binding sites with narrow peaks (100-1,000 bp).
The context information provided by the five neighbouring residues on each side of the target residue was previously shown to be optimal for sequence-based prediction of DNA-binding residues [ 9, 10].
Furthermore, a "Goldilocks zone" must exist for each protein where the actin-binding affinity must be optimal for accumulation.
You might sum it up as classical liberal holism: what is optimal for one must be optimal for all.
Using a synthetic TZF domain peptide derived from the human TTP, known as TTP73, our group independently showed that this same nonamer sequence was optimal for TTP binding on gel-shift analysis, which could be accomplished with binding affinities in the low nanomolar range [ 31].
