title: Towards Understanding Protein Disorder In-Cell.
abstract: Investigating the activity and structure of cellular biochemical machinery at atomic resolution has been a point of paramount significance for understanding health and disease over the decades. The underlying molecular mechanisms are primarily studied in vitro. Nuclear magnetic resonance (NMR) is a technique that allows to look into cells and study proteins and other constituents, thanks to careful experimental design and technological advances (spectrometer sensitivity and pulse sequence design). Here we outline current applications of the technique and propose a realistic future for the field.
authors.affiliation: VIB Department of Structural Biology, Vrije Universiteit Brussel, 1050, Brussels, Belgium.
authors.forename: Cesyen
authors.initials: C
authors.lastname: Cedeño
authors.affiliation: BioTalentum Ltd, Aulich L. str. 26, 2100, Godollo, Hungary.
authors.forename: Hadas
authors.initials: H
authors.lastname: Raveh-Hamit
authors.affiliation: BioTalentum Ltd, Aulich L. str. 26, 2100, Godollo, Hungary. andras.dinnyes@biotalentum.hu.
authors.forename: András
authors.initials: A
authors.lastname: Dinnyés
authors.affiliation: VIB Department of Structural Biology, Vrije Universiteit Brussel, 1050, Brussels, Belgium.|Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518, Budapest, Hungary.
authors.forename: Peter
authors.initials: P
authors.lastname: Tompa
mesh_terms: D004926:Escherichia coli / Q000737:chemistry*; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: Cell extracts; Cell types; In-cell NMR; Isotopic labeling