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N‐terminal acetylation is critical for forming α‐helical oligomer of α‐synuclein
Author(s) -
Trexler Adam J.,
Rhoades Elizabeth
Publication year - 2012
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2056
Subject(s) - tetramer , oligomer , acetylation , monomer , biophysics , chemistry , terminal (telecommunication) , dimer , alpha synuclein , protein aggregation , protein structure , biochemistry , biology , disease , parkinson's disease , enzyme , medicine , computer science , polymer chemistry , telecommunications , organic chemistry , pathology , gene , polymer
The aggregation of the protein α‐synuclein (AS) is critical to the pathogenesis of Parkinson's disease. Although generally described as an unstructured monomer, recent evidence suggests that the native form of AS may be an α‐helical tetramer which resists aggregation. Here, we show that N‐terminal acetylation in combination with a mild purification protocol results in an oligomeric form of AS with partial α‐helical structure. N‐terminal acetylation of AS could have important implications for both the native and pathological structures and functions of AS. Through our demonstration of a recombinant expression system, our results represent an important step toward biochemical and biophysical characterization of this potentially important form of AS.