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Biochemistry|October 6, 1987
Phosphorescence anisotropy of liver alcohol dehydrogenase in the crystalline state. Apparent glasslike rigidity of the coenzyme-binding domainG B Strambini, E GabellieriBiophysical Journal|February 1, 1996
Proteins in frozen solutions: evidence of ice-induced partial unfoldingG B Strambini, E GabellieriEuropean Journal of Biochemistry|April 1, 1994
Conformational changes in proteins induced by dynamic associations. A tryptophan phosphorescence studyE Gabellieri, G B StrambiniBiochemistry|January 10, 1989
Phosphorescence properties and protein structure surrounding tryptophan residues in yeast, pig, and rabbit glyceraldehyde-3-phosphate dehydrogenaseG B Strambini, E GabellieriBiophysical Journal|April 28, 2001
Structural perturbations of azurin deposited on solid matrices as revealed by trp phosphorescenceE Gabellieri, G B StrambiniPhotochemistry and Photobiology|June 1, 1990
Temperature dependence of tryptophan phosphorescence in proteinsG B Strambini, E GabellieriBiophysical Chemistry|July 1, 1989
Phosphorescence properties of Trp-84 and Trp-310 in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilusE Gabellieri, G B StrambiniBiophysical Chemistry|May 1, 1988
Tryptophan phosphorescence and the conformation of liver alcohol dehydrogenase in solution and in the crystalline stateE Gabellieri, G B Strambini, P GualtieriThe Biochemical Journal|November 14, 1997
Modification of the mitochondrial F1-ATPase epsilon subunit, enhancement of the ATPase activity of the IF1-F1 complex and IF1-binding dependence of the conformation of the epsilon subunitG Solaini, A Baracca, E Gabellieri, et al.The Journal of Biological Chemistry|September 15, 1995
Conformational changes of the mitochondrial F1-ATPase epsilon-subunit induced by nucleotide binding as observed by phosphorescence spectroscopyA Baracca, E Gabellieri, S Barogi, et al.Pageof 3