On the problem of resonance assignments in solid state NMR of uniformly ¹⁵N,¹³C-labeled proteins.

ABSTRACT: Determination of accurate resonance assignments from multidimensional chemical shift correlation spectra is one of the major problems in biomolecular solid state NMR, particularly for relative large proteins with less-than-ideal NMR linewidths. This article investigates the difficulty of resonance assignment, using a computational Monte Carlo/simulated annealing (MCSA) algorithm to search for assignments from artificial three-dimensional spectra that are constructed from the reported isotropic (15)N and (13)C chemical shifts of two proteins whose structures have been determined by solution NMR methods. The results demonstrate how assignment simulations can provide new insights into factors that affect the assignment process, which can then help guide the design of experimental strategies.

SUBMITTER: Tycko R 

PROVIDER: S-EPMC4371143 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature