Sequence-specific Ni(II)-dependent peptide bond hydrolysis for protein engineering. Combinatorial library determination of optimal sequences.

By A. Krężel, Edyta Kopera, A. Protas, J. Poznański, A. Wysłouch-Cieszyńska, W. Bal. 2010

57 citations recorded by the source corpus.

Subfields: Molecular Biology

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In Molecular Biology

1. W. Bal
2. Edyta Kopera
3. Agnieszka Belczyk-Ciesielska
4. Mariusz Jaskolski

Citations in the corpus

• Atomic Resolution Structure of a Protein Prepared by Non-Enzymatic His-Tag Removal. Crystallographic and NMR Study of GmSPI-2 Inhibitor (2014, background): “Our previous studies demonstrated that Ni(II) ions hydrolyze the peptide bond preceding the serine or threonine residue in (S/ T)XHZ peptide sequences [12].”
• Application of Ni(II)-Assisted Peptide Bond Hydrolysis to Non-Enzymatic Affinity Tag Removal (2012, methodology): “In order to verify the biotechnological applicability of this Ni(II)assisted reaction we use the recombinant SPI2 protein extended C-terminally by the SRHWAP-His6 dodecapeptide, which comprises the best Ni(II)-sensitive tetrapeptide (SRHW), obtained by peptide library screening [16], linked to the H”