Martina Huber

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a-Synuclein (as) is a 140-residue protein abundantly present in the Lewy bodies characteristic of Parkinson's disease.[1-31 It is a member of the class of intrinsically disordered proteins (lOPs) that have unusual properties and whose physiological relevance is becoming increasingly recognized.[41 lOPs lack a well-defined three-dimensional fold and display(More)
α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson's disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved(More)
alpha-Synuclein (alphaS) is the main component of Lewy bodies from Parkinson's disease. That alphaS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of alphaS sheds light on the most likely structure. For alphaS bound to vesicles large enough to accommodate also the extended(More)
The Parkinson's disease-related protein alpha-Synuclein (alphaS) is a 140 residue intrinsically disordered protein. Its membrane-binding properties are thought to be relevant for its physiological or pathologic activity. Here, the interaction of alphaS with POPG [1-Palmitoyl-2-Oleoyl-sn-Glycero-3-(Phosphorac-(1-glycerol))] small unilamellar vesicles (SUVs)(More)
Binding of human α-Synuclein, a protein associated with Parkinson's disease, to natural membranes is thought to be crucial in relation to its pathological and physiological function. Here the binding of αS to small unilamellar vesicles mimicking the inner mitochondrial and the neuronal plasma membrane is studied in situ by continuous wave and pulsed(More)
Introduction Alpha-synuclein The human a-synuclein protein (ASYN) plays a central role in the etiology of Parkinson's disease,llI and forms fibrillar aggregates that are found in Lewy bodies and Lewy neurites in the brain, structures which are the hallmark of the diseaseY-4 1 Three point mutations (A30P, AS3T, and E46K)1 are associated with early-onset(More)
The structure and function of membrane proteins is partly determined by the interaction of these proteins with the lipids of the membrane. Peptides forming single membrane-spanning alpha-helices, such as the WALP peptide (acetyl-GWWL(AL)(n)WWA-amide), are good models for such interactions. This interaction can be studied by investigating the aggregation of(More)
Cytochrome f (Cyt f) and plastocyanin (Pc) form a highly transient complex as part of the photosynthetic redox chain. The complex from Nostoc sp. PCC 7119 was studied by NMR relaxation spectroscopy with the aim of determining the orientation of Pc relative to Cyt f. Chemical-shift-perturbation analysis showed that the presence of spin labels on the surface(More)
The amyloid β (A β) peptide is important in the context of Alzheimer's disease, since it is one of the major components of the fibrils that constitute amyloid plaques. Agents that can influence fibril formation are important, and of those, membrane mimics are particularly relevant, because the hydrophobic part of A β suggests a possible membrane activity of(More)
Understanding the functioning of ion channels, as well as utilizing their properties for biochemical applications requires control over channel activity. Herein we report a reversible control over the functioning of a mechanosensitive ion channel by interfering with its interaction with the lipid bilayer. The mechanosensitive channel of large conductance(More)