Title : The conformation and the aggregation kinetics of α-synuclein depend on the proline residues in its C-terminal region.

Pub. Date : 2010 Nov 2

PMID : 20828147






3 Functional Relationships(s)
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1 For this purpose, we produced and purified His-WT alpha-syn, a recombinant alpha-syn with a polyhistidine tag (six His residues) and a linker, and a number of Pro-to-Ala mutants. Histidine synuclein alpha Homo sapiens
2 Finally, we show that the mutant of His alpha-syn with all five proline residues mutated to alanine is more structured (more alpha-helix) than His-WT alpha-syn, indicating the role of the Pro residues as potential helix breakers in the inhibitory conformation of the C-terminus. Histidine synuclein alpha Homo sapiens
3 Finally, we show that the mutant of His alpha-syn with all five proline residues mutated to alanine is more structured (more alpha-helix) than His-WT alpha-syn, indicating the role of the Pro residues as potential helix breakers in the inhibitory conformation of the C-terminus. Histidine synuclein alpha Homo sapiens