Current approaches for the study of large proteins by NMR

Journal Article (Journal Article)

An overview of current methods employed for characterizing larger (>25 kDa) proteins by NMR is presented. These techniques include: the attenuation of T2 relaxation effects by offsetting dipole-dipole and chemical shift anisotropy relaxation mechanisms (TROSY); the extraction of residual dipolar couplings from partially oriented molecules; the elimination of relaxation pathways by incorporating deuterium nuclei into protein samples; the easing of resonance overlap by isotopically labeling only specific protein segments; and the decrease of rotational correlation times by dissolving proteins in low viscosity solvents. © 2002 Elsevier Science B.V. All rights reserved.

Full Text

Duke Authors

Cited Authors

  • Venters, RA; Thompson, R; Cavanagh, J

Published Date

  • January 9, 2002

Published In

Volume / Issue

  • 602-603 /

Start / End Page

  • 275 - 292

International Standard Serial Number (ISSN)

  • 0022-2860

Digital Object Identifier (DOI)

  • 10.1016/S0022-2860(01)00690-1

Citation Source

  • Scopus