Alpha synuclein beta sheet structure

The term secondary structure refers to the interaction of the hydrogen bond donor and acceptor residues of the repeating peptide unit. The two most important secondary structures of proteins, the alpha helix and the beta sheet, were predicted by the American chemist Linus Pauling in the early 1950s.

Dec 05, 2019 · The alpha-synuclein proteins of all aggregates contain beta sheets, which is in line with previous investigations. Accordingly, the molecular backbone is twisted in a way that the proteins are ...

Celej MS, Sarroukh R, Goormaghtigh E et al (2012) Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure. Biochem J 443:719–726 CrossRef PubMed Google Scholar Jul 11, 2019 · Besides fibrils, alpha-synuclein exists in other structural forms, including an orderly stacked form called beta-sheet. To date, not much is known about which of alpha-synuclein’s structural arrangements contribute more strongly to disease mechanisms and Parkinson’s manifestations. Jan 22, 2013 · Parkinson's Disease (PD) is an age-related deterioration of dopaminergic neurons in the substantia nigra and other brain regions. The pathological hallmark of PD is the cytoplasmic deposition of amyloid-like aggregates termed Lewy Bodies , the fibrous inclusions which contain the protein α-Synuclein (α-Syn) [1–3]. α-Syn is a soluble, natively unfolded protein containing 140 a.a. which is ... Jun 24, 2008 · The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative diseases. In Parkinson's disease it is believed that the aggregation of α-synuclein (α-syn) from monomers by intermediates into amyloid fibrils is the toxic disease-causative mechanism. Here, we studied ... The misfolded alpha-Synuclein, rich in beta-sheet structure (shown in red) can be the precursor of aggregation. The illustration depicts steps of self propagation of alpha-Synuclein from misfolded monomers->oligomers->fibrils->Lewy bodies.

Alpha-Synuclein Amyloid Oligomers Exhibit Beta-Sheet Antiparallel Structure as Revealed by FTIR Spectroscopy Article in Biophysical Journal 102(3):440- · January 2012 with 208 Reads Academia.edu is a platform for academics to share research papers. SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1. Academia.edu is a platform for academics to share research papers. The term secondary structure refers to the interaction of the hydrogen bond donor and acceptor residues of the repeating peptide unit. The two most important secondary structures of proteins, the alpha helix and the beta sheet, were predicted by the American chemist Linus Pauling in the early 1950s. Fibrillar alpha-synuclein with the distinctive cross-beta sheet structure of amyloid is a major component of Lewy bodies (Spillantini et al., 1997; Serpell et al., 2000). Using existing techniques, detection of Parkinson’s disease pathology is largely limited to lesions that occur late in the disease, including Lewy bodies, in degenerating ...