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PubMed · 17046391

Protein aggregation starting from the native globular state.

Giordana Marcon·Georgia Plakoutsi·Fabrizio Chiti
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Abstract

Amyloid formation by globular proteins that normally adopt a compact folded structure is generally induced in vitro under harsh conditions involving low pH, high temperature, high pressure, or in the presence of organic solvents. Under these conditions, folded proteins are generally unfolded, at least partially. The approach described here shows a rationale and two detailed examples as to how the mechanism of aggregation of a globular protein can be probed under conditions in which it is initially in its folded conformation, and hence relevant to a physiological environment.

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Acid Anhydride HydrolasesBacterial ProteinsCarboxyl and Carbamoyl TransferasesEscherichia coli ProteinsHumansKineticsProtein ConformationProtein FoldingProtein Structure, QuaternaryProteinsSulfolobus solfataricusAcylphosphataseJournal Article

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Giordana Marcon, Georgia Plakoutsi, Fabrizio Chiti. 2006. Protein aggregation starting from the native globular state.. https://doi.org/10.1016/s0076-6879(06)13004-9

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