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Protein Science : a Publication of the Protein Society|July 28, 1999
Equilibrium unfolding of a small low-potential cytochrome, cytochrome c553 from Desulfovibrio vulgarisP Wittung-StafshedeBiochimica Et Biophysica Acta|April 16, 1998
A stable, molten-globule-like cytochrome cP Wittung-StafshedeBiochimica Et Biophysica Acta|July 17, 1999
Effect of redox state on unfolding energetics of heme proteinsP Wittung-StafshedeBiochemistry|November 7, 2001
Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurinI Pozdnyakova, P Wittung-StafshedeJournal of Molecular Biology|September 1, 2000
Cytochrome c(553), a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kineticsJ Guidry, P Wittung-StafshedeFEBS Letters|June 10, 1996
Redox-linked conformational changes in cytochrome c oxidaseP Wittung, B G MalmströmBiochemistry|July 1, 1997
Extended DNA-recognition repertoire of peptide nucleic acid (PNA): PNA-dsDNA triplex formed with cytosine-rich homopyrimidine PNAP Wittung, P Nielsen, B NordénEuropean Journal of Biochemistry|August 15, 1994
Spectroscopic observation of renaturation between polynucleotides with RecA in the presence of ATP hydrolysisP Wittung, B Nordén, M TakahashiEuropean Journal of Biochemistry|February 15, 1995
Secondary structure of RecA in solution. The effects of cofactor, DNA and ionic conditionsP Wittung, B Nordén, M TakahashiBiochimica Et Biophysica Acta|June 23, 2000
No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxinD Apiyo, J Guidry, P Wittung-StafshedePageof 5