Hemoglobin allostery

Ackers, G. (1998), Deciphering the molecular code of hemoglobin allostery , in Di Cera (Ed ), Advances in Protein Chemistry, Vol. 51, Linkage Thermodynamics of Macromolecular Interactions, Academic Press, San Diego, CA, pp. 185-253... 

Alternative models for hemoglobin allostery, (a) In the symmetry model hemoglobin can exist in only two states. (b) In the sequential model hemoglobin can exist in a number of different states. Only the subunit binding oxygen must be in the high-affinity form. 

Goldbeck RA, Esquerra RM, Holt JM, Ackers GK, Kliger DS. The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relations. Biochemistry 2004 43 12048-12064. 

GK. Ackers. 1998. Deciphering the molecular code of hemoglobin allostery At/v. Protein Chem. 51 185-253. (PubMed)... 

See also Models of Allosteric Activity, Hemoglobin Allostery... 

See also Hemoglobin Allostery, The Bohr Effect, Carbon Dioxide and Hemoglobin, Bisphosphoglycerate and Hemoglobin... 

Allostery Hemoglobin is an allosteric protein. This means that the binding of 02 to one... 

Describe the concept of allostery as it applies to hemoglobin and to regulatory enzymes. 

To begin, we will consider the principles of allostery by examining two proteins the enzyme aspartate transcarhamoylase and the oxygen-transporting protein hemoglobin. 

An illustration of the probable nonadaptive origin of allostery is furnished by the wrapping of hemoglobin across orthologs in species with vastly different population size. Thus, this protein becomes richer in dehydrons and more prone to oligomerization in species with smaller population, with the majority of the new dehydrons located at the interface that promotes the quaternary structure of the homomer (Fig. 6.1c). 

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