High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy

High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2008-06, Vol.3 (6), p.e2359-e2359
Main Authors: Korukottu, Jegannath, Schneider, Robert, Vijayan, Vinesh, Lange, Adam, Pongs, Olaf, Becker, Stefan, Baldus, Marc, Zweckstetter, Markus
Format: Article
Language:English
Subjects:
Amyloid
Atomic structure
Biology
Biophysics
Biophysics/Experimental Biophysical Methods
Biophysics/Membrane Proteins and Energy Transduction
Biophysics/Structural Genomics
Chemistry
Crystallography
Experiments
High resolution
Magnetic resonance spectroscopy
Mathematical analysis
Membrane proteins
Models, Molecular
Molecular Structure
NMR spectroscopy
Nuclear magnetic resonance spectroscopy
Potassium
Protein structure
Proteins
Scorpion Venoms - chemistry
Solid state
Spectroscopy
X-ray crystallography
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:High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0002359