Conformation change of α-synuclein(61-95) at the air-water interface and quantitative measurement of the tilt angle of the axis of its α-helix by multiple angle incidence resolution spectroscopy
Abstract
Various techniques have been developed to determine protein's structure to understand how proteins work. Compared with X-ray crystallography requiring proteins to form single crystal structure and NMR which usually needs long time measurement, surface FT-IR techniques are able to quickly determine the tilt angle (the key information to determine whether the α-helix is transmembrane) of peptides/proteins in a monolayer at the interface (e.g. membranes). Specifically, for α-helical peptides/proteins in membrane, the tilt angle of the axis is one of the key information. In this paper, Multiple Angle Incidence Resolution Spectroscopy (MAIRS), a recently developed surface FTIR technique, was applied for the first time to quantitatively determine the tilt angle of the axis of α-helical model peptide related to α-synuclein (α-syn). α-Syn is a 140-amino-acid presynaptic protein whose aggregation is the hallmark of Parkinson's disease (PD). It is difficult for α-syn to form a single crystal structure and the primary structure of α-syn constitutes three domains: the N-terminus containing residues 1-60; the nonamyloid component (NAC) which spans residues 61-95 and is highly prone to aggregation; and C-terminus with residues 96-140. Here,...Continue Reading
References
Inter-helix distances in lysophospholipid micelle-bound alpha-synuclein from pulsed ESR measurements
Citations
Related Concepts
Related Feeds
Alpha-Synuclein Aggregation (MDS)
Alpha-synucleins are small proteins that are believed to restrict the mobility of synpatic vesicles and inhibit neurotransmitter release. Aggregation of these proteins have been linked to several types of neurodegenerative diseases including dementia with Lewy bodies and Parkinson's disease. Here is the latest research on α-synuclein aggregation.