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G Irace

Showing results (1-10 of 66) with videos related to

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International Journal of Peptide and Protein Research|November 1, 1988
Protein conformational changes induced by guanidine at predenaturational concentrationsE Bismuto, G Irace
Journal of Molecular Biology|August 5, 1994
Unfolding pathway of apomyoglobin. Simultaneous characterization of acidic conformational states by frequency domain fluorometryE Bismuto, G Irace
FEBS Letters|December 26, 2001
The effect of molecular confinement on the conformational dynamics of the native and partly folded state of apomyoglobinE Bismuto, G Irace
Biochemistry|December 26, 1978
Thyroxine-induced conformational changes in prealbuminG Irace, H Edelhoch
Biochimica Et Biophysica Acta|October 20, 1975
Covalent structure of fibrinopeptides from buffaloes breeding in ItalyC Balestrieri, G Colonna, G Irace
Biochimica Et Biophysica Acta|February 12, 2000
Tryptophanyl contributions to apomyoglobin fluorescence resolved by site-directed mutagenesisI Sirangelo, S Tavassi, G Irace
Bollettino Della Societa Italiana Di Biologia Sperimentale|July 25, 2000
Single tryptophanyl substitutions affect the structure of apomyoglobinI Sirangelo, S Tavassi, G Irace
Biochemistry|August 30, 1983
Unfolding pathway of myoglobin. Evidence for a multistate processE Bismuto, G Colonna, G Irace
Biochemistry|March 22, 1988
Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobinE Bismuto, E Gratton, G Irace
Biochemistry|February 21, 1989
Multiple conformational states in myoglobin revealed by frequency domain fluorometryE Bismuto, G Irace, E Gratton
Pageof 7

Showing results (1-10 of 66) with videos related to

Sort By:
Pageof 7
International Journal of Peptide and Protein Research|November 1, 1988
Protein conformational changes induced by guanidine at predenaturational concentrationsE Bismuto, G Irace
Journal of Molecular Biology|August 5, 1994
Unfolding pathway of apomyoglobin. Simultaneous characterization of acidic conformational states by frequency domain fluorometryE Bismuto, G Irace
FEBS Letters|December 26, 2001
The effect of molecular confinement on the conformational dynamics of the native and partly folded state of apomyoglobinE Bismuto, G Irace
Biochemistry|December 26, 1978
Thyroxine-induced conformational changes in prealbuminG Irace, H Edelhoch
Biochimica Et Biophysica Acta|October 20, 1975
Covalent structure of fibrinopeptides from buffaloes breeding in ItalyC Balestrieri, G Colonna, G Irace
Biochimica Et Biophysica Acta|February 12, 2000
Tryptophanyl contributions to apomyoglobin fluorescence resolved by site-directed mutagenesisI Sirangelo, S Tavassi, G Irace
Bollettino Della Societa Italiana Di Biologia Sperimentale|July 25, 2000
Single tryptophanyl substitutions affect the structure of apomyoglobinI Sirangelo, S Tavassi, G Irace
Biochemistry|August 30, 1983
Unfolding pathway of myoglobin. Evidence for a multistate processE Bismuto, G Colonna, G Irace
Biochemistry|March 22, 1988
Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobinE Bismuto, E Gratton, G Irace
Biochemistry|February 21, 1989
Multiple conformational states in myoglobin revealed by frequency domain fluorometryE Bismuto, G Irace, E Gratton
Pageof 7