Erratum to: Fluorescence Quenching to Study Protein-ligand Binding: Common Errors
β Scribed by Marco van de Weert
- Book ID
- 106413150
- Publisher
- Springer
- Year
- 2011
- Tongue
- English
- Weight
- 44 KB
- Volume
- 21
- Category
- Article
- ISSN
- 1053-0509
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A Readily Reproducible Collection Of Established And Emerging Techniques For Studying The Interaction Between Proteins And Ligands, Including Biochemical/bulk Techniques, Structure Analysis, Spectroscopy, Single-molecule Studies, And Theoretical/computational Tools. Among The Highlights Are Surface
When a polypeptide binds to DNA, the rotational mobility of a chromophore on the polypeptide is reduced. This simple fact makes it feasible to use polarization of fluorescence methods to study polypeptide-nucleic acid interaction. Previous (l-3) polarization of fluorescence studies of polypeptide-DN