3D HCCH-COSY-TOCSY experiment for the assignment of ribose and amino acid side chains in (13)C labeled RNA and protein Journal Article


Authors: Hu, W.; Kakalis, L. T.; Jiang, L.; Jiang, F.; Ye, X.; Majumdar, A.
Article Title: 3D HCCH-COSY-TOCSY experiment for the assignment of ribose and amino acid side chains in (13)C labeled RNA and protein
Abstract: A new 3D HCCH-COSY-TOCSY experiment is presented for the assignment of RNA sugar and protein side chains. The experiment, which combines COSY and TOCSY units, is more powerful than the sum of individual HCCH-COSY and HCCH-TOCSY pulse sequences. The experiment was applied to a 13C, 15N-labeled 26 mer RNA complexed with the antibiotic tobramycin, and a 12 kDa 13C, 15N-labeled FKBP12 protein sample. The power of HCCH-COSY-TOCSY is demonstrated through complete spin system assignments of sugars in the 26 mer RNA sample, which could not be assigned using a combination of HCCH-COSY, HCCH-TOCSY and 13C-edited NOESY experiments.
Keywords: methodology; protein conformation; proteins; protein; rna; chemistry; nucleotide sequence; base sequence; binding site; amino acid; binding sites; amino acids; conformation; nucleic acid conformation; tobramycin; nuclear magnetic resonance; immunophilin; carbon; carbon isotopes; nuclear magnetic resonance, biomolecular; ribose; peptidylprolyl isomerase; fk 506 binding protein; oligoribonucleotide; oligoribonucleotides; tacrolimus binding proteins; article; immunophilins; assignment; hcch-cosy-tocsy; side chain
Journal Title: Journal of Biomolecular NMR
Volume: 12
Issue: 4
ISSN: 0925-2738
Publisher: Springer  
Date Published: 1998-01-01
Start Page: 559
End Page: 564
Language: English
PUBMED: 9862131
PROVIDER: scopus
DOI: 10.1023/a:1008365301124
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
Altmetric
Citation Impact
BMJ Impact Analytics
MSK Authors
  1. Feng Jiang
    13 Jiang
  2. Weidong Hu
    16 Hu
  3. Xiao Mei Ye
    6 Ye