Principles of Medical Biochemistry: With STUDENT CONSULT by Gerhard Meisenberg PhD, William H. Simmons PhD

By Gerhard Meisenberg PhD, William H. Simmons PhD

"Highly Commended," simple and scientific Sciences type, British scientific organization 2012 clinical ebook Competition

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In many cases these mutations lead to overproduction of Ab-42. The development of drugs that inhibit b-secretase or shift the cleavage specificity of gsecretase away from the formation of Ab-42 has not yet been successful, and Alzheimer disease still is incurable. 16 Degradation of b-amyloid precursor protein (APP). A, Cleavage by a-secretase followed by g-secretase produces only innocuous products. B, Cleavage by b-secretase followed by g-secretase produces b-amyloid. In Alzheimer disease, b-amyloid polymerizes into aggregates and eventually forms insoluble fibrils.

A, Cleavage by a-secretase followed by g-secretase produces only innocuous products. B, Cleavage by b-secretase followed by g-secretase produces b-amyloid. In Alzheimer disease, b-amyloid polymerizes into aggregates and eventually forms insoluble fibrils. AICD, b-Amyloid precursor protein intracellular domain. 27 28 PRINCIPLES OF MOLECULAR STRUCTURE AND FUNCTION killing the neurons. Because the brain has little extracellular space, most of these protein deposits are intracellular, and they do not always have the classic amyloid structure.

Why? Completely deoxygenated hemoglobin is mainly in the T conformation, which has a very low oxygen affinity. This accounts for the flat part of the curve below about 10 torr. However, with increasing oxygen partial pressure, the first heme nevertheless becomes oxygenated. Oxygenation of the first heme destabilizes the T conformation and shifts the structure toward the R conformation. This repeats itself after binding of the second and third oxygen molecules. Oxygen binding to a heme group in hemoglobin increases the oxygen affinities of the remaining heme groups.

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