2014/02/25 by Luke Edwards, Luke J. Edwards, D. V. Savostyanov +5 · 46 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #Advanced NMR Techniques and Applications #Chemical physics #Chemistry #Condensed matter physics #J-coupling #Molecular physics #Nuclear magnetic resonance #Nuclear magnetic resonance spectroscopy #Physics #Protein Structure and Dynamics #Quantum #Quantum decoherence #Quantum many-body systems #Quantum mechanics #Relaxation (psychology) #Spectroscopy #Spin (aerodynamics) #Spin engineering #Spin polarization #Spins #Statistical physics #Thermodynamics #Two-dimensional nuclear magnetic resonance spectroscopy #physics.chem-ph #quant-ph
paper · pdf · doi:10.1016/j.jmr.2014.04.002
published in Journal of Magnetic Resonance 243, 107-113 (Elsevier BV) · Submitted for publication
arxiv created 2014/02/25 · openalex publication_date 2014/04/18 · arxiv updated 2014/07/16 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
Nuclear magnetic resonance spectroscopy is one of the few remaining areas of physical chemistry for which polynomially scaling quantum mechanical simulation methods have not so far been available. In this communication we adapt the restricted state space approximation to protein NMR spectroscopy and illustrate its performance by simulating common 2D and 3D liquid state NMR experiments (including accurate description of relaxation processes using Bloch-Redfield-Wangsness theory) on isotopically enriched human ubiquitin - a protein containing over a thousand nuclear spins forming an irregular polycyclic three-dimensional coupling lattice. The algorithm uses careful tailoring of the density operator space to only include nuclear spin states that are populated to a significant extent. The reduced state space is generated by analysing spin connectivity and decoherence properties: rapidly relaxing states as well as correlations between topologically remote spins are dropped from the basis set.