View Single Post
  #1  
Unread 08-22-2010, 03:41 AM
nmrlearner's Avatar
nmrlearner nmrlearner is offline
Senior Member
 
Join Date: Jan 2005
Posts: 23,135
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 Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignme

Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignments by two-dimensional NMR.

Related Articles Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignments by two-dimensional NMR.

Biochim Biophys Acta. 1995 Apr 27;1248(2):177-85

Authors: Shao W, Liu G, Tang W

The binding of 1-methylimidazole to the heme iron by displacing Met-80 of cytochrome c has been studied by two-dimensional (2D) exchange spectroscopy. Two components of cytochrome c ligated by 1-methylimidazole (1-MeIm-cyt c) are first identified, which are related to the sterically hindered orientation of 1-methylimidazole by the heme pocket. Based on a matrix formalism, the kinetic parameters are calculated from the 2D peak amplitudes. With the known resonance assignments of cytochrome c, some hyperfine shifted resonances arising from heme peripheral protons and two axial ligands, and some side-chain resonances of the aliphatic and aromatic protons of 1-MeIm-cyt c have been straightforwardly assigned, which provide a clue to ligand-induced electronic and molecular structural changes of the protein.

PMID: 7748900 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No