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Allostery is an intrinsic property of many globular proteins and enzymes that is indispensable for cellular regulatory and feedback mechanisms. Recent theoretical and empirical observations indicate that allostery is also manifest in intrinsically disordered proteins, which account for a substantial proportion of the proteome. Many intrinsically disordered(More)
We combined rapid microfluidic mixing with single-molecule fluorescence resonance energy transfer to study the folding kinetics of the intrinsically disordered human protein α-synuclein. The time-resolution of 0.2 ms revealed initial collapse of the unfolded protein induced by binding with lipid mimics and subsequent rapid formation of transient structures(More)
a-Synuclein is an abundant presynaptic protein that is associated with several biological activities, including vesicle trafficking, [1] maintenance of synaptic SNARE complexes and vesicle pools, [2, 3] and regulation of dopamine metabolism. [4] The protein is believed to play a central role in the patho-genesis of Parkinsons disease (PD), as evidenced by(More)
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