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J A Schauerte

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

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Biochemistry|May 2, 1989
Long-lived tryptophan fluorescence in phosphoglycerate mutaseJ A Schauerte, A Gafni
Biochemical and Biophysical Research Communications|July 26, 1995
Photodegradation of tryptophan residues and attenuation of molecular chaperone activity in alpha-crystallin are correlatedJ A Schauerte, A Gafni
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1992
Time-resolved circularly polarized protein phosphorescenceJ A Schauerte, D G Steel, A Gafni
Methods in Enzymology|January 1, 1997
Time-resolved room temperature tryptophan phosphorescence in proteinsJ A Schauerte, D G Steel, A Gafni
Biophysical Journal|April 1, 1996
Improved differentiation between luminescence decay components by use of time-resolved optical activity measurements and selective lifetime modulationJ A Schauerte, A Gafni, D G Steel
Biochemistry|April 19, 2000
Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterasesA Gershenson, J A Schauerte, L Giver, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 17, 1995
Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenaseJ A Schauerte, B D Schlyer, D G Steel, et al.
Biophysical Journal|September 1, 1994
Time-resolved room temperature protein phosphorescence: nonexponential decay from single emitting tryptophansB D Schlyer, J A Schauerte, D G Steel, et al.
Biochimica Et Biophysica Acta|May 9, 2001
Differences in the pathways for unfolding and hydrogen exchange among mutants of Escherichia coli alkaline phosphataseC J Fischer, J A Schauerte, K C Wisser, et al.
Biochemistry|February 24, 2000
Hydrogen exchange at the core of Escherichia coli alkaline phosphatase studied by room-temperature tryptophan phosphorescenceC J Fischer, J A Schauerte, K C Wisser, et al.
Pageof 1

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

Sort By:
Pageof 1
Biochemistry|May 2, 1989
Long-lived tryptophan fluorescence in phosphoglycerate mutaseJ A Schauerte, A Gafni
Biochemical and Biophysical Research Communications|July 26, 1995
Photodegradation of tryptophan residues and attenuation of molecular chaperone activity in alpha-crystallin are correlatedJ A Schauerte, A Gafni
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1992
Time-resolved circularly polarized protein phosphorescenceJ A Schauerte, D G Steel, A Gafni
Methods in Enzymology|January 1, 1997
Time-resolved room temperature tryptophan phosphorescence in proteinsJ A Schauerte, D G Steel, A Gafni
Biophysical Journal|April 1, 1996
Improved differentiation between luminescence decay components by use of time-resolved optical activity measurements and selective lifetime modulationJ A Schauerte, A Gafni, D G Steel
Biochemistry|April 19, 2000
Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterasesA Gershenson, J A Schauerte, L Giver, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 17, 1995
Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenaseJ A Schauerte, B D Schlyer, D G Steel, et al.
Biophysical Journal|September 1, 1994
Time-resolved room temperature protein phosphorescence: nonexponential decay from single emitting tryptophansB D Schlyer, J A Schauerte, D G Steel, et al.
Biochimica Et Biophysica Acta|May 9, 2001
Differences in the pathways for unfolding and hydrogen exchange among mutants of Escherichia coli alkaline phosphataseC J Fischer, J A Schauerte, K C Wisser, et al.
Biochemistry|February 24, 2000
Hydrogen exchange at the core of Escherichia coli alkaline phosphatase studied by room-temperature tryptophan phosphorescenceC J Fischer, J A Schauerte, K C Wisser, et al.
Pageof 1