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Biochemistry|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 GonnelliBiochemistry|October 24, 1995
Phosphorescence lifetime of tryptophan in proteinsM Gonnelli, G B StrambiniBiophysical Chemistry|March 15, 2001
No effect of trimethylamine N-oxide on the internal dynamics of the protein native foldM Gonnelli, G B StrambiniBiophysical Chemistry|July 1, 1986
The rate of equine liver alcohol dehydrogenase denaturation by urea. Dependence on temperature and denaturant concentrationM Gonnelli, G B StrambiniBiochemistry|January 24, 1998
Time-resolved protein phosphorescence in the stopped-flow: denaturation of horse liver alcohol dehydrogenase by urea and guanidine hydrochlorideM Gonnelli, G B StrambiniBiophysical Journal|July 1, 1993
Glycerol effects on protein flexibility: a tryptophan phosphorescence studyM Gonnelli, G B StrambiniJournal of Fluorescence|November 19, 2013
Tryptophan phosphorescence of ribonuclease T1 as a probe of protein flexibilityM Gonnelli, A Puntoni, G B StrambiniBiochemistry|January 9, 1990
Room temperature phosphorescence of Trp-314 as a monitor of subunit communications in alcohol dehydrogenase from horse liverG B Strambini, M Gonnelli, W C GalleyBiophysical Chemistry|September 1, 1994
Heterogeneity of protein conformation in solution from the lifetime of tryptophan phosphorescenceP Cioni, E Gabellieri, M Gonnelli, et al.Pageof 5