Hemoglobin fundamental

Isotherm Subtraction. A second method (7) of determining the net proton coefficient from adsorption data is an adaptation of the thermodynamics of linked functions as applied to the binding of gases to hemoglobin (19). The net proton coefficient determined by this method is designated, Xp- The computational procedure makes a clear distinction between the influence of adsorption density and pH on the magnitude of the net proton coefficient. The fundamental equation used in the calculation of Xp is... 

Primary structure is the amino / ) acid sequence, which controls the shape of the protein and the role the protein serves in the body. Primary Structure Primary structure is the most fundamental of the four structural levels because it is the protein s amino acid sequence that determines its overall shape and function. So crucial is primary structure to function that the change of only one amino acid out of several hundred can drastically alter biological properties. The disease sickle-cell anemia, for example, is caused by a genetic defect in blood hemoglobin whereby valine is substituted for glutamic add at only one position in a chain of 146 amino acids. 

In natural systems, redox proteins such as cytochrome c (cyt c) function not only to transfer electrons, but to transfer electrons specifically to a particular redox partner, usually another macromolecule. Transfer of electrons between subunits of modified hemoglobins and within complexes of cyt c with cyt b5 and cyt c with cyt c peroxidase (Cep) have therefore been studied extensively (41,42). These studies have revealed the fundamental requirements for the recognition process leading to the formation of the protein-protein complex as well as the thermodynamic features of the electron-transfer reaction itself. This reaction, outlined in equation 6, consists of three fundamental processes recognition to form a complex (Ki), electron transfer within the complex, and dissociation of the redox-altered complex (K2). For the cyt c-Ccp complex, Fe(II) cyt c corresponds to P2red and oxidized Cep corresponds to P °x. 

In his scheme representing the development of heme proteins, Ingram (1961) has also anticipated that myoglobin may be the fundamental structure from which the chains of both normal and pathological hemoglobins were formed. 

This volume has been written for those chemists and biochemists who may never themselves do X-ray diffraction analyses of crystals, but who need to be able to understand the results of such studies on structures of immediate interest to them. The fields of structural biology and chemistry have blossomed in the years since X-ray diffraction was discovered in 1912. For example, the three-dimensional structures of benzene, graphite, the alkali halides, the boron hydrides, the rare gas halides, penicillin, vitamin Bjj, hemoglobin, lysozyme, transfer RNA, and the common-cold rhinovirus have been determined and, in each case, the results have greatly increased our understanding of fundamental chemistry and biochemistry. 

The fundamental quantity to be used in any standardized spectro-photometric determination of hemoglobin should be the quarter millimolar extinction coefficient because of the four Fe atoms per hemoglobin molecule. This quantity is independent of the molecular weight of hemoglobin. Consequently, a redetermination of the molecular weight will not change the value of the extinction coefficient to be used and will not affect hemoglobin concentrations when these are expressed in quarter millimoles per liter. 

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