Structural Studies of Autophagy-Related Proteins.
Animals
Autophagy-Related Proteins
/ chemistry
Cryopreservation
/ methods
Cryoprotective Agents
/ chemistry
Crystallization
/ methods
Crystallography, X-Ray
/ methods
Humans
Molecular Dynamics Simulation
Nuclear Magnetic Resonance, Biomolecular
/ methods
Protein Conformation
Software
Vesicular Transport Proteins
/ chemistry
MD simulation
NMR spectroscopy
X-ray crystallography
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2019
2019
Historique:
entrez:
6
1
2019
pubmed:
6
1
2019
medline:
25
6
2019
Statut:
ppublish
Résumé
Information about the structure and dynamics of proteins is crucial for understanding their physiological functions as well as for the development of strategies to modulate these activities. In this chapter we will describe the work packages required to determine the three-dimensional structures of proteins involved in autophagy by using X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Further we will provide instructions how to perform a molecular dynamics (MD) simulation using GABARAP as example protein.
Identifiants
pubmed: 30610688
doi: 10.1007/978-1-4939-8873-0_2
doi:
Substances chimiques
ATG101 protein, human
0
Autophagy-Related Proteins
0
Cryoprotective Agents
0
Vesicular Transport Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM