Three-Dimensional Triple-Resonance NMR of ¹³C/¹⁵N-Enriched Proteins Using Constant-Time Evolution

Authors

Robert Powers, University of Nebraska - LincolnFollow
Angela M. Gronenborn, Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland
G. Marius Clore, Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland
Ad Bax, Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland

Document Type

Article

Date of this Version

1991

Citation

Journal of Magnetic Resonance 94, 209-213 ( 1991 )

Comments

U.S. Government Work

Abstract

Recently it has been convincingly demonstrated that 30 triple-resonance NMR provides a practical alternative for obtaining sequential resonance assignments in larger proteins ( 1, 2). This approach requires a set of five or six 30 NMR experiments that correlate the various protein backbone nuclei. Details regarding the mechanisms and technical implementations of these experiments have been described previously ( 3- 5). Two of the experiments used in this approach correlate backbone Hα and Cα resonances with either the intraresidue carbonyl resonance (CO) or the ¹⁵N resonance of the succeeding residue and are referred to as HCACO and HCA(CO)N, respectively. The present Communication describes a modification of these experiments which optimizes their sensitivity and removes the F₁ antiphase character of correlations.