4D solid-state NMR for protein structure determination

Solid-state NMR offers the chance to extend structural studies to proteins that are otherwise difficult to study at atomic resolution, such as protein fibrils, membrane proteins or poorly diffracting crystals. As two-dimensional spatial correlation NMR spectra of proteins suffer from severe resonanc...

Full description

Saved in:
Bibliographic Details
Published in:Physical chemistry chemical physics : PCCP 2012-04, Vol.14 (15), p.5239-5246
Main Authors: Huber, Matthias, Bckmann, Anja, Hiller, Sebastian, Meier, Beat H
Format: Article
Language:English
Subjects:
Atomic structure
Chemistry
Colloidal state and disperse state
Crystal structure
Diffraction
Exact sciences and technology
General and physical chemistry
Mathematical analysis
Membranes
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Tertiary
Proteins
Proteins - chemistry
Protons
Spectra
Three dimensional
Ubiquitin - chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Solid-state NMR offers the chance to extend structural studies to proteins that are otherwise difficult to study at atomic resolution, such as protein fibrils, membrane proteins or poorly diffracting crystals. As two-dimensional spatial correlation NMR spectra of proteins suffer from severe resonance overlap, we analyze in this perspective article the potential of higher-dimensional (3D and 4D) proton-detected experiments, which have an increased number of identifiable and assignable distance restraints for solid-state structural studies. We discuss practical considerations for the NMR measurements and the preparation of suitable protein samples and show results of structure calculations from 4D solid-state NMR spectra. 3D- and 4D proton-detected spatial correlation spectra from perdeuterated proteins with 1 H amide and methyl labels yield unambiguous distance restraints for structural studies by solid-state NMR.
ISSN:1463-9076
1463-9084
DOI:10.1039/c2cp23872a