Riboflavin binding (or carrier) protein (RfBP) is a monomeric, two-domain protein, originally purified from hens' egg white. RfBP contains nine disulfide bridges; as a result, the protein forms a compact structure and undergoes reversible three-state thermal denaturation. This was demonstrated using
β¦ LIBER β¦
Binding Study of Riboflavin-Binding Protein with Riboflavin and Its Analogues by Differential Scanning Calorimetry
β Scribed by Marcin Wasylewski
- Book ID
- 111563176
- Publisher
- Springer
- Year
- 2000
- Tongue
- English
- Weight
- 46 KB
- Volume
- 19
- Category
- Article
- ISSN
- 1573-4943
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Evaluation of riboflavin binding protein
β
Marcin Wasylewski
π
Article
π
2004
π
Elsevier Science
π
English
β 173 KB
Electrochemistry of riboflavin-binding p
β
Martin BartoΕ‘Γk; Veronika OstatnΓ‘; Emil PaleΔek
π
Article
π
2009
π
Elsevier Science
π
English
β 362 KB
Femtosecond Fluorescence Dynamics of Fla
β
Mataga, Noboru; Chosrowjan, Haik; Taniguchi, Seiji; Tanaka, Fumio; Kido, Nobuo;
π
Article
π
2002
π
American Chemical Society
π
English
β 80 KB
Two-dimensional differential scanning ca
β
Martin Straume; Ernesto Freire
π
Article
π
1992
π
Elsevier Science
π
English
β 728 KB
A general theoretical development for the design and analysis of two-dimensional thermal stability surfaces of proteins is presented. The surfaces are generated from multiple excess heat capacity profiles ( vs T) obtained at varying concentrations of an interacting ligand. The energetics of both the
Interaction of Resveratrol and Its Trime
β
Sarpietro, Maria Grazia; Spatafora, Carmela; Tringali, Corrado; Micieli, Dorotea
π
Article
π
2007
π
American Chemical Society
π
English
β 185 KB
The study of growth inhibitive protein f
β
Marina D. Rukhadze; Diana V. Dzidziguri; Nana M. Giorgobiani; Salome M. Kerkenji
π
Article
π
2005
π
John Wiley and Sons
π
English
β 92 KB
π 1 views