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Biochemistry|September 24, 1996
Effects of NAD+ binding on the luminescence of tryptophans 84 and 310 of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilusE Gabellieri, S Rahuel-Clermont, G Branlant, et al.Biophysical Journal|June 23, 1998
Tyrosine quenching of tryptophan phosphorescence in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilusG B Strambini, E Gabellieri, M Gonnelli, et al.Biophysical Journal|July 1, 1983
Singular oxygen effects on the room-temperature phosphorescence of alcohol dehydrogenase from horse liverG B StrambiniBiophysical Journal|July 1, 1987
Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structureG B StrambiniBiochemistry|May 6, 1986
Effects of urea and guanidine hydrochloride on the activity and dynamical structure of equine liver alcohol dehydrogenaseG B Strambini, M GonnelliBiochemistry|January 9, 1990
Tryptophan luminescence from liver alcohol dehydrogenase in its complexes with coenzyme. A comparative study of protein conformation in solutionG B Strambini, M GonnelliJournal of Molecular Biology|May 5, 1989
Dynamical structure of glutamate dehydrogenase as monitored by tryptophan phosphorescence. Signal transmission following binding of allosteric effectorsP Cioni, G B StrambiniBiochemistry|October 24, 1995
Phosphorescence lifetime of tryptophan in proteinsM Gonnelli, G B StrambiniBiochemistry|July 15, 1997
Pressure-induced dissociation of yeast glyceraldehyde-3-phosphate dehydrogenase: heterogeneous kinetics and perturbations of subunit structureP Cioni, G B StrambiniJournal of Molecular Biology|August 24, 1999
Pressure/temperature effects on protein flexibilty from acrylamide quenching of protein phosphorescenceP Cioni, G B StrambiniPageof 6