title: Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes.
abstract: Aggregates formed by amyloidogenic peptides and proteins and reconstituted membrane protein preparations differ significantly in terms of the spectral quality that they display in solid-state NMR experiments. Structural heterogeneity and dynamics can both in principle account for that observation. This perspectives article aims to point out challenges and limitations, but also potential opportunities in the investigation of these systems.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave, Boston, MA, 02115, USA.
authors.forename: Rasmus
authors.initials: R
authors.lastname: Linser
authors.forename: Riddhiman
authors.initials: R
authors.lastname: Sarkar
authors.forename: Alexey
authors.initials: A
authors.lastname: Krushelnitzky
authors.forename: Andi
authors.initials: A
authors.lastname: Mainz
authors.forename: Bernd
authors.initials: B
authors.lastname: Reif
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012995:Solubility
chemical_list: D000682:Amyloid; D008565:Membrane Proteins; D046912:Multiprotein Complexes; D011506:Proteins