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Disulfide exchange folding of insulin-like growth factor I.
Hober S, Forsberg G, Palm G, Hartmanis M, Nilsson B. Hober S, et al. Biochemistry. 1992 Feb 18;31(6):1749-56. doi: 10.1021/bi00121a024. Biochemistry. 1992. PMID: 1737028
In a separate experiment, early refolding intermediates were trapped by pyridylethylation after only 90 s of refolding in the glutathione buffer, starting from reduced IGF-I. ...
In a separate experiment, early refolding intermediates were trapped by pyridylethylation after only 90 s of refolding in the glutath …
Stability towards alkaline conditions can be engineered into a protein ligand.
Gülich S, Linhult M, Nygren P, Uhlén M, Hober S. Gülich S, et al. J Biotechnol. 2000 Jun 23;80(2):169-78. doi: 10.1016/s0168-1656(00)00259-5. J Biotechnol. 2000. PMID: 10908797
Charge engineering of a protein domain to allow efficient ion-exchange recovery.
Gräslund T, Lundin G, Uhlén M, Nygren PA, Hober S. Gräslund T, et al. Protein Eng. 2000 Oct;13(10):703-9. doi: 10.1093/protein/13.10.703. Protein Eng. 2000. PMID: 11112509
Strategy for highly selective ion-exchange capture using a charge-polarizing fusion partner.
Gräslund T, Ehn M, Lundin G, Hedhammar M, Uhlén M, Nygren PA, Hober S. Gräslund T, et al. J Chromatogr A. 2002 Jan 4;942(1-2):157-66. doi: 10.1016/s0021-9673(01)01413-3. J Chromatogr A. 2002. PMID: 11822381
Engineering streptococcal protein G for increased alkaline stability.
Gülich S, Linhult M, Ståhl S, Hober S. Gülich S, et al. Protein Eng. 2002 Oct;15(10):835-42. doi: 10.1093/protein/15.10.835. Protein Eng. 2002. PMID: 12468718
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