Previously we demonstrated for several examples that peptides having a general internal
sequence RN-Yaa-Ser/Thr-Xaa-His-Zaa-RC (Yaa= Glu or Ala, Xaa= Ala or His, Zaa= Lys …

In previous studies we showed that Ni (II) ions can hydrolytically cleave a peptide bond
preceding Ser/Thr in peptides of a general sequence RN–(Ser/Thr)–Xaa–His–Zaa–RC …

Recently we screened a combinatorial library of R1-(Ser/Thr)-Xaa-His-Zaa-R2 peptides
(Xaa= 17 common α-amino acids, except Asp, Glu, and Cys; Zaa= 19 common α-amino …

Previously we demonstrated the sequence-specific hydrolysis of the R1-(Ser/Thr)-peptide
bond in Ni (II) complexes of peptides with a general R1-(Ser/Thr)-Xaa-His-Zaa-R2 sequence …

Previously we demonstrated that Ni (II) complexes of Ac-Thr-Glu-Ser-His-His-Lys-NH2
hexapeptide, representing residues 120-125 of human histone H2A, and some of its …

Recently, we described a sequence-specific R1-(Ser/Thr) peptide bond hydrolysis reaction
in peptides of a general sequence R1–(Ser/Thr)–Xaa–His–Zaa–R, which occurs in the …

The total chemical synthesis of proteins has great potential for increasing our understanding
of the molecular basis of protein function. The introduction of native chemical ligation …

A method for solid-phase peptide synthesis in the N-to C-direction that delivers good
coupling yields and a low degree of epimerization is reported. The optimized method …

A novel strategy in kinetically controlled enzymatic peptide synthesis is described. Various
amino acid derivatives with charged, highly solubilizing Nα-protecting groups were prepared …

A conformationally purified peptide library was constructed based on a unique idea
combining the combinatorial library concept with de novo peptide design. This peptide …