Hemoglobin structure-function relationship

Hemoglobin Structure-Function Relationship by the Use of the Generalized Adair Equation... 

The structure-function relationship of hemoglobin in solution at atomic resolution 04CRV1219. 

R 21 J.A. Lukin and C. Ho, The Structure-Function Relationship of Hemoglobin in Solution at Atomic Resolution , p. 1219... 

HEMOGLOBIN OXYGEN BINDING, ERYTHROCYTE SHAPE TRANSFORMATIONS, AND MODELING OF CELL DIFFERENTIATION AS EXAMPLES OF THEORETICAL APPROACHES IN STUDYING THE STRUCTURE-FUNCTION RELATIONSHIP IN BIOLOGICAL SYSTEMS... 

As a prerequisite to the determination of the quantitative structure-function relationship it is necessary to define the parameters with which the system of hemoglobin and its ligands is described at the thermodynamic level. The ligand binding curve expresses the thermodynamic properties of the system at equilibrium and therefore this discussion is limited to the thermodynamic equilibrium. 

A proposal will be made here that in some specific cases the GAE represents a suitable way for the study of the structure-function relationship in the hemoglobin system. Before proceeding to put forward this proposal a short critical account on the modeling usually used in discussions relating the structure and function of this system will be presented. 

The interest in the structure-function relationship in hemoglobin has been primarily focused on the molecular mechanism of the cooperative oxygen binding. The main relevant structural information related to this problem was the differences observed between the oxy and deoxy structures of hemoglobin. However, little is known about the structure of the intermediately oxygenated hemoglobin molecules. Several models have therefore been proposed in order to... 

Stefano Bettati received his MS degree from the University of Parma in 1992, defending a thesis on The allosteric regulation of the enzyme tryptophan synthase, and his Ph.D. degree in 1998 from the University of Modena, by working on hemoglobin. He was a postdoctoral fellow at the laboratory of Chemical Physics, National Institutes of Health, Bethesda, MD, USA, from 1999 to 2000. At present he is a full professor at Applied Physics, Faculty of Medicine, University of Parma, Italy. His current research interests are mainly in structure, function, and dynamics relationships of PLP-dependent enzymes, heme proteins, and green fluorescent proteins. 

Despite all these studies of proteins and synthetic models, many essential aspects of the function of myoglobin and hemoglobin, e.g. the way the protein controls the binding of ligands (02, CO, and NO), the precise structure of the Fe-ligand bonds and the structure-spin-energy relationships at the active center, are a topic of debate [2]. 

The diseases and disorders chosen for discussion and the order of presentation parallel subject matter taught in most first-year medical biochemistry. Chapters in the first part of the book, Nucleic Acids and Protein Structure, illustrate the relationships of protein structure and function with respect to collagen (Osteogenesis Imperfecta) and hemoglobin (Sickle Cell Anemia). The chapters Fragile X Syndrome and Hereditary Spherocytosis discuss key aspects of DNA and protein structure and their respective role in chromosomal and cytoskeletal structure. The chapter cardiac troponin and myocardial infarction provides an up-to-date demonstration of the usefulness of both structural proteins and enzymes as markers of cardiovascular disease, while the chapter cx Anti trypsin Deficiency discusses the important role of endogenous enzyme inhibitors. 

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