The Quaternary Structure of Bovine alpha-Crystallin. Surface Probing by Limited Proteolysis in vitro
نویسندگان
چکیده
منابع مشابه
Probing protein structure by limited proteolysis.
Limited proteolysis experiments can be successfully used to probe conformational features of proteins. In a number of studies it has been demonstrated that the sites of limited proteolysis along the polypeptide chain of a protein are characterized by enhanced backbone flexibility, implying that proteolytic probes can pinpoint the sites of local unfolding in a protein chain. Limited proteolysis ...
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Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...
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alpha-Crystallin has been shown to function as a molecular chaperone in preventing thermal aggregation of crystallins and other proteins. The molecular mechanism of this protection is not yet clear. gamma-Crystallin aggregates upon exposure to UV light. We have investigated the effect of the presence of alpha-crystallin in the photoaggregation process and find that alpha-crystallin does not pre...
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The quaternary structure of alpha-crystallin is dynamic, a property which has thwarted crystallographic efforts towards structural characterization. In this study, we have used collision-induced dissociation mass spectrometry to examine the architecture of the polydisperse assemblies of alpha-crystallin. For total alpha-crystallin isolated directly from fetal calf lens using size-based chromato...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb13055.x