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A designed metal-binding protein with a novel fold.
Pessi A, Bianchi E, Crameri A, Venturini S, Tramontano A, Sollazzo M. Pessi A, et al. Among authors: bianchi e. Nature. 1993 Mar 25;362(6418):367-9. doi: 10.1038/362367a0. Nature. 1993. PMID: 8455724
Affinity purification of a difficult-sequence protein. Implications for the inclusion of capping in synthetic protocols.
Bianchi E, Sollazzo M, Tramontano A, Pessi A. Bianchi E, et al. Int J Pept Protein Res. 1993 Jul;42(1):93-6. Int J Pept Protein Res. 1993. PMID: 8370647
A biotinylated derivative of a designed, difficult-sequence protein (the Minibody, Bianchi, E., Tramontano, A., Sollazzo, M. & Pessi, A. (1993) Int. J. Peptide Protein Res. 41, 385-393) which represented only 3.7% of the crude, cleaved material was quantitativel …
A biotinylated derivative of a designed, difficult-sequence protein (the Minibody, Bianchi, E., Tramontano, A., Sollazzo, M. & …
Surface topology of Minibody by selective chemical modifications and mass spectrometry.
Zappacosta F, Ingallinella P, Scaloni A, Pessi A, Bianchi E, Sollazzo M, Tramontano A, Marino G, Pucci P. Zappacosta F, et al. Among authors: bianchi e. Protein Sci. 1997 Sep;6(9):1901-9. doi: 10.1002/pro.5560060911. Protein Sci. 1997. PMID: 9300490 Free PMC article.
This is also in agreement with previous results that were obtained using a similar approach where mass spectrometry was used to identify Minibody fragments from limited proteolysis (Zappacosta F, Pessi A, Bianchi E, Venturini S, Sollazzo M, Tramontano A. Marino G, P …
This is also in agreement with previous results that were obtained using a similar approach where mass spectrometry was used to identify Min …
907 results