Cooperative binding systems are being studied taking into account site or subunit interactions, ligand interactions, aggregation and redistribution in proteins and model systems. Methods are being developed to evaluate reasonable parameters describing these reactions. We study amino acids and proteins where the number of sites is small, and also those systems such as the protein-DNA complex and the helix-coil transition where the number of sites can be very large. An additional system where the number of sites is large is that involved in the subunit interactions of proteins. The interactions between the four subunits of hemoglobin can now be studied in detail. Five sets of X'ray data on the structure of human deoxy hemoglobin A now reside in the Brookhaven data banks. These data are being analyzed to define the nature of the interactions in the dimer interface of deoxy hemoglobin. Interactions in this interface constitute the main source of the cooperativity on the binding of oxygen to hemoglobin.
| Saroff, Harry A (2004) pH effects on the binding of oxygen to non-vertebrate monomeric hemoglobins. A linked function model. J Theor Biol 229:113-8 |
| Saroff, Harry A (2003) Structure of deoxyhemoglobin: ionizable groups and polyethylene glycol. Proteins 50:329-40 |
