This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.The majority of physicochemical studies on highly purified proteins has been performed in non-interactive (dilute) conditions. These conditions are often far from actual cytosolic conditions. For instance, the extremely high physiological concentration (350mg/ml) of alpha-crystalline and its repulsive interaction potential are a key to the transparency of the eye lens, as proven by a series of SAXS studies in late 1970?s and 1980?s. Another concentrated condition of high medical importance exists in erythrocytes. The physiological hemoglobin concentration in adult human erythrocyte is in excess of 300mg/ml. Most other proteins would easily associate with each other non-specifically and precipitate in this concentration range. The electrostatic properties of hemoglobin (Hb) allow it to be highly soluble and maintain low cytosol viscosity to allow deformation of erythrocyte to pass though microscopic blood vessels. A single amino acid mutation of hemoglobin is known to cause sickled-cell anemia among a sizable world population, including a fraction of the US population. Sickle hemoglobin (HbS) polymerizes in erythrocytes and causes the hardening of the cell wall, thus interfering smooth passage in blood vessels. We have initiated SAXS studies on human Hb to obtain base line information in preparation for studies of HbS.
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