Titlebook: GAPDH: Biological Properties and Diversity; Norbert W. Seidler Book 2013 The Editor(s) (if applicable) and The Author(s), under exclusive

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Agronomy

Dynamic Oligomeric Properties,ctural basis that underlies the conformational sub-states of the GAPDH oligomer is discussed. The issue of protein stability is given a thorough analysis, since it is well-established that the primary strategy for protein oligomerization is to stabilize conformation. Several factors that affect olig

BILL

Multiple Binding Partners,eracting molecules grouped into specific functional and structural categories. By organizing the binding partners in this way, certain common structural features are beginning to surface, such as acidic dipeptide sequences that are found in several of these binding proteins. Additionally, the consen

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https://doi.org/10.1007/978-3-658-30614-4xperimental analysis of GAPDH’s enzymatic function, particularly in the use of inhibitors. The GAPDH gene is portrayed in the context of the enzyme’s role in metabolism. The observed intolerance to genetic mutation suggests that the genetic changes (i.e. those seen across species) may provide a trea

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ACE-inhibitor

Die Gesetze von Angebot und Nachfragen meeting focal energy demands, this chapter discusses several other very distinct GAPDH functions (i.e. membrane fusogenic properties) that are quite different from its ability to catalyze oxidative phosphorylation of the triose, glyceraldehyde 3-phosphate. It is suggested that a single protein par

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