Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures.

ABSTRACT: While low-temperature Nuclear Magnetic Resonance (NMR) holds great promise for the analysis of unstable samples and for sensitizing NMR detection, spectral broadening in frozen protein samples is a common experimental challenge. One hypothesis explaining the additional linewidth is that a variety of conformations are in rapid equilibrium at room temperature and become frozen, creating an inhomogeneous distribution at cryogenic temperatures. Here, we investigate conformational heterogeneity by measuring the backbone torsion angle (Ψ) in Escherichia coli Dihydrofolate Reductase (DHFR) at 105 K. Motivated by the particularly broad N chemical shift distribution in this and other examples, we modified an established NCCN Ψ experiment to correlate the chemical shift of N_i+1 to

SUBMITTER: Yi X 

PROVIDER: S-EPMC10895356 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature