Based on the crystal dimeric structure of HLA-DR molecules, we designed, and synthesized molecules able to induce the putative coreceptors dimerization.
To investigate the precise localization of cytoplasmic γ actin in skeletal muscle and the relationship to dystrophin molecules, we designed an antibody against the N-terminal peptide of cytoplasmic γ actin.
Based on the crystal structure of HLA-class II molecules we designed and synthesized a cyclic analog with restricted conformation, cyclo(Suc-Thr-Pro-Gln-Arg-Gly-Asp-Val-Lys -Thr-OH (Suc-Thr-Pro-Gln-Arg-Gly-Asp-Val-Lys -Thr-OHn with a Suc-Thr-Pro-Gln-Arg-Gly-Asp-Val-Lys -Thr-OH
Since the SYFPEITHI program only predicts binding of 15 amino acid sequences to HLA-DR molecules, we designed longer peptides by adding flanking residues in both ends that resulted in overlapping multiple epitopes for CD4 (15 amino acids) within one sequence.
To further test that (a) all the proteins used initially have encapsulated within the nanogel network and (b) the β-thiopropionate linker is responsible for the release of the encapsulated protein molecules, we designed and synthesized a control nanogel using a cross-linker that lacks β-thiopropionate functional group.
To study S1 at a single-molecule level, we designed nanoparticle conjugates making use of the strong biotin-streptavidin interaction.
The molecules we design every day are just a sample which we hope will help to contribute for a better tomorrow'.
By introducing an additional H-bond in the α1β2 subunit interface or altering the charge properties of the amino acid residues in the α1β1 subunit interface of the hemoglobin molecule, we have designed and expressed recombinant hemoglobins (rHbs) with low oxygen affinity and high cooperativity.
As a continuity of our ongoing effort to identify novel small-molecule LSD1-inhibitors, we designed and synthesized a series of resveratrol derivatives, which were shown to be potent inhibitors of LSD1.
To determine the intracellular distribution of Hfq molecules by EM, we designed an Hfq-MT fusion protein and expressed it in E. coli.
