Faculty Opinions recommendation of Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences.

Author(s):  
John Ladbury
Cell ◽  
1994 ◽  
Vol 78 (4) ◽  
pp. 603-615 ◽  
Author(s):  
Siu-Kwong Chan ◽  
Leah Jaffe ◽  
Maria Capovilla ◽  
Juan Botas ◽  
Richard S. Mann

Biochemistry ◽  
2004 ◽  
Vol 43 (14) ◽  
pp. 4170-4178 ◽  
Author(s):  
Jon C. D. Houtman ◽  
Yuichiro Higashimoto ◽  
Nazzareno Dimasi ◽  
Sangwoo Cho ◽  
Hiroshi Yamaguchi ◽  
...  

2016 ◽  
Vol 30 (8) ◽  
pp. 927-934 ◽  
Author(s):  
Inbal Marcu ◽  
David Oppenheim ◽  
Nina Koren-Karie

1970 ◽  
Vol 65 (1_Suppl) ◽  
pp. S104-S121 ◽  
Author(s):  
E. E. Baulieu ◽  
J. P. Raynaud ◽  
E. Milgrom

ABSTRACT A brief review of the characteristics of steroid binding proteins found in the plasma and in some target organs is presented, followed by some general remarks on binding »specificity« and binding parameters. Useful techniques for measuring binding parameters at equilibrium are reported, both those which keep the equilibrium intact and those which implicate its disruption. A concept is developed according to which the determination of a specific steroid binding protein is based on the »differential dissociation« of the several steroid binding complexes present in most biological mixtures. Methods which allow determination of the kinetic parameters of the binding systems are also presented. Various representations of the binding and therefore different modes of graphic representation and calculation are discussed, including the recent »proportion graph« method.


Sign in / Sign up

Export Citation Format

Share Document