Thread: NMR paper Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of
View Single Post
  #1  
Unread 08-22-2010, 03:50 AM
nmrlearner's Avatar
nmrlearner nmrlearner is offline
Senior Member
  
Join Date: Jan 2005
Posts: 23,187
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 0
Downloads: 0
Uploads: 0
Default Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of
Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.

Related Articles Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.

Toxicol Lett. 1995 Dec;82-83:577-89

Authors: Hsu VL, Jia X, Kearns DR

The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to resonance overlap and broadened crosspeaks. This approach involved the use of selectively deuteriated, 13C- and 15N-labeled samples and 'isotopic heterodimers' to distinguish between intra- and intermonomeric NOEs. A comparison with the crystal structure and NMR analysis of the E. coli HU protein suggests that other homologous proteins in this family will possess similar tertiary structures. This NMR strategy is applicable to the study of other proteins and their biomolecular complexes.

PMID: 8597113 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote

Did you find this post helpful? Yes | No