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Biochimica Et Biophysica Acta|February 12, 2000
Tryptophanyl contributions to apomyoglobin fluorescence resolved by site-directed mutagenesisI Sirangelo, S Tavassi, G IraceBollettino Della Societa Italiana Di Biologia Sperimentale|July 25, 2000
Single tryptophanyl substitutions affect the structure of apomyoglobinI Sirangelo, S Tavassi, G IraceBiochimica Et Biophysica Acta|March 14, 1993
Folding and dynamics of melittin in reversed micellesE Bismuto, I Sirangelo, G IraceArchives of Biochemistry and Biophysics|November 15, 1991
Conformational dynamics of unfolded peptides as a function of chain length: a frequency domain fluorescence approachE Bismuto, I Sirangelo, G IraceFEBS Letters|January 24, 1994
Solvent and thermal denaturation of the acidic compact state of apomyoglobinI Sirangelo, E Bismuto, G IracePhotochemistry and Photobiology|June 1, 1994
Resolution of the individual tryptophanyl contributions to the near-ultraviolet dichroic activity of apomyoglobinI Sirangelo, G Irace, E BismutoBiophysical Chemistry|September 1, 1992
Fluorescence lifetime distribution of 1,8-anilinonaphthalenesulfonate (ANS) in reversed micelles detected by frequency domain fluorometryE Bismuto, I Sirangelo, G IraceArchives of Biochemistry and Biophysics|November 1, 1992
Salt-induced refolding of myoglobin at acidic pH: molecular properties of a partly folded intermediateE Bismuto, I Sirangelo, G IraceBiochemistry|September 19, 1989
Conformational substates of myoglobin detected by extrinsic dynamic fluorescence studiesE Bismuto, I Sirangelo, G IraceBollettino Della Societa Italiana Di Biologia Sperimentale|August 22, 2001
Role of tryptophanyl residues in driving myoglobin foldingI Sirangelo, M Casillo, C Malmo, et al.Pageof 2