Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules

Lars Sonnenberg; Sorin Luca; Marc Baldus

doi:10.1016/j.jmr.2003.10.014

Multiple-spin analysis of chemical-shift-selective (13C, 13C) transfer in uniformly labeled biomolecules

J Magn Reson. 2004 Jan;166(1):100-10. doi: 10.1016/j.jmr.2003.10.014.

Authors

Lars Sonnenberg¹, Sorin Luca, Marc Baldus

Affiliation

¹ Department for NMR-Based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

PMID: 14675825
DOI: 10.1016/j.jmr.2003.10.014

Abstract

Chemical-shift-selective (13C, 13C) polarization transfer is analyzed in uniformly labeled biomolecules. It is shown that the spin system dynamics remain sensitive to the distance of interest and can be well reproduced within a quantum-mechanical multiple-spin analysis. These results lead to a general approach on how to describe chemical-shift-selective transfer in uniformly labeled systems. As demonstrated in the case of ubiquitin, this methodology can be used to detect long-range distance constraints in uniformly labeled proteins.

Publication types

Comparative Study
Evaluation Study
Research Support, Non-U.S. Gov't
Validation Study

MeSH terms

Biopolymers / analysis
Biopolymers / chemistry*
Carbon Isotopes*
Computer Simulation
Crystallography / methods*
Histidine / analysis
Histidine / chemistry*
Hydrochloric Acid / analysis
Hydrochloric Acid / chemistry
Isotope Labeling / methods*
Magnetic Resonance Spectroscopy / methods*
Models, Molecular*
Molecular Conformation
Protein Conformation
Spin Labels
Ubiquitin / analysis
Ubiquitin / chemistry*

Substances

Biopolymers
Carbon Isotopes
Spin Labels
Ubiquitin
Histidine
Hydrochloric Acid