Probing Structural Changes in Alpha-Synuclein by Nuclear Magnetic Resonance Spectroscopy. Academic Article uri icon

Overview

abstract

  • Alpha-synuclein, the principal protein involved in the pathogenesis of Parkinson's disease, has been shown to exchange between multiple conformational states, with hitherto unclear physiological role of such conformational changes. Due to its ability to provide rich structural information for proteins in their near-native environment, nuclear magnetic resonance (NMR) spectroscopy has been a valuable tool to study these conformational states. In this review we describe the application of model systems and NMR methods to the study of membrane-bound states of alpha-synuclein. We provide a detailed description, primarily meant for someone new to the field, of how to prepare the necessary samples, perform the basic experiments, and obtain an initial interpretation of the results.

publication date

  • January 1, 2019

Research

keywords

  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • alpha-Synuclein

Identity

PubMed Central ID

  • PMC8193918

Scopus Document Identifier

  • 85061594265

Digital Object Identifier (DOI)

  • 10.1007/978-1-4939-9124-2_13

PubMed ID

  • 30771177

Additional Document Info

volume

  • 1948