Literature DB >> 22052493

The morpheein model of allostery: evaluating proteins as potential morpheeins.

Eileen K Jaffe1, Sarah H Lawrence.   

Abstract

An equilibrium mixture of alternate quaternary structure assemblies can form a basis for allostery. The morpheein model of allostery is a concerted dissociative model that describes an equilibrium of alternate quaternary structure assemblies whose architectures are dictated by alternate conformations in the dissociated state. Kinetic and biophysical anomalies that suggest that the morpheein model of allostery applies for a given protein of interest are briefly described. Two methods are presented for evaluating proteins as potential morpheeins. One is a subunit interchange method that uses chromatography, dialysis, and mass spectroscopy to monitor changes in multimer composition. The other is a two-dimensional native gel electrophoresis method to monitor ligand-induced changes in an equilibrium of alternate multimeric assemblies.

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Year:  2012        PMID: 22052493      PMCID: PMC3256758          DOI: 10.1007/978-1-61779-334-9_12

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  26 in total

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8.  Kinetics and thermodynamics of the interchange of the morpheein forms of human porphobilinogen synthase.

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5.  wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs.

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