Thread: NMR paper In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-reson
View Single Post
  #1  
Unread 08-22-2010, 02:20 PM
nmrlearner's Avatar
nmrlearner nmrlearner is offline
Senior Member
  
Join Date: Jan 2005
Posts: 23,188
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 In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-reson
In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.

Related Articles In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.

Arch Biochem Biophys. 1996 Sep 1;333(1):221-4

Authors: Klug CA, Burzio LA, Waite JH, Schaefer J

Rotational-echo double-resonance (REDOR) 13C NMR spectra with 2H dephasing have been obtained from plaques and threads from the byssus of the marine mussel Mytilus edulis labeled by sea-water exposure to L-[ring-4-(13)C]tyrosine and L-[ring-d4]tyrosine for 2 days. Specific isotopic enrichment of tyrosine in protein reached 25% in both 13C and 2H. Fifteen percent of the total 13C label was incorporated as diphenolic carbon. Based on REDOR dephasing, about one-tenth of tyrosine rings in both intact plaques and threads are within 4 A of each other or rings of 3,4-dihydroxy-phenylalanine (DOPA). However, there is no direct evidence for the formation of covalent linkages between or among tyrosine and DOPA rings in either plaques or threads.

PMID: 8806774 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote

Did you find this post helpful? Yes | No