Streptavidin cooperative allosterism upon binding biotin observed by differential changes in intrinsic fluorescence-Reference-Cited by-同舟云学术

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Streptavidin cooperative allosterism upon binding biotin observed by differential changes in intrinsic fluorescence

Published:2019-03 Issue: Volume:17 Page:127-131
ISSN:2405-5808
Container-title:Biochemistry and Biophysics Reports
language:en
Short-container-title:Biochemistry and Biophysics Reports

Author:

Waner Mark J.,Hiznay James M.,Mustovich Anthony T.,Patton William,Ponyik Charles,Mascotti David P.

Funder

The John Carroll University College of Arts & Sciences

The Camille and Henry Dreyfus Foundation, Inc.

Publisher

Elsevier BV

Subject

Biochemistry,Biophysics

Reference27 articles.

1. Nonspecific ligand-DNA equilibrium binding parameters determined by fluorescence methods;Lohman;Methods Enzymol.,1992

2. Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding;Lohman;Methods Enzymol.,1991

3. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic method for assessing the quaternary state and comparative thermostability of avidin and streptavidin - Bayer - - - Wiley online library;Bayer;Electrophoresis,1996

4. Extremely high thermal stability of streptavidin and avidin upon biotin binding;González;Biomol. Eng.,1999

5. Isolation and properties of streptavidin;Bayer;Methods Enzymol.,1990

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