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News Physiol Sci 18: 232-236, 2003; doi:10.1152/nips.01451.2003
1548-9213/03 $5.00
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News in Physiological Sciences, Vol. 18, No. 6, 232-236, December 2003
© 2003 Int. Union Physiol. Sci./Am. Physiol. Soc.

Allosteric Proteins: Lessons to be Learned From the Hemoglobin Intermediates

Michele Perrella and Rosaria Russo

Dipartimento di Scienze e Tecnologie Biomediche, Università di Milano, I-20090 Segrate (MI), Italy
Allosteric proteins, such as hemoglobin, are assemblies of functional units, which undergo quaternary structural transitions in response to concentration changes of a specific ligand. Functional properties of hemoglobin ligation intermediates indicate that the tertiary structural changes induced by the ligand do not promote an equilibrium of quaternary structures.






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