Interaction of Mn2+ with DNA as studied by proton-relaxation enhancement of solvent water

Biopolymers ◽  
1981 ◽  
Vol 20 (5) ◽  
pp. 915-923 ◽  
Author(s):  
Raymond Van Steenwinkel ◽  
Francesco Campagnari ◽  
Margaret Merlini
Keyword(s):  
Proton Relaxation ◽  
Solvent Water ◽  
Proton Relaxation Enhancement

74. PROTON RELAXATION ENHANCEMENT IN TISSUE DUE TO INGESTED MnC12

1984 ◽  
Vol 19 (5) ◽  
pp. S19
Author(s):  
A. C. Mamourian ◽  
K. R. Burnett ◽  
G. L. Wolf ◽  
E. J. Goldstein ◽  
H. Y. Kressel ◽  
...  
Keyword(s):  
Proton Relaxation ◽  
Proton Relaxation Enhancement

Proton relaxation enhancement

1993 ◽  
Vol 3 (1) ◽  
pp. 149-156 ◽  
Author(s):  
Michael L. Wood ◽  
Peter A. Hardy
Keyword(s):  
Proton Relaxation ◽  
Proton Relaxation Enhancement

Proton relaxation enhancement (PRE) in biochemistry: A critical survey

1979 ◽  
Vol 13 (1) ◽  
pp. 1-45 ◽  
Author(s):  
Dennis R. Burton ◽  
Sture Forsen ◽  
Gunnar Karlstrom ◽  
Raymond A. Dwek
Keyword(s):  
Proton Relaxation ◽  
Critical Survey ◽  
Proton Relaxation Enhancement

Effects of spatial distribution on proton relaxation enhancement by particulate iron oxide

1994 ◽  
Vol 4 (5) ◽  
pp. 653-657 ◽  
Author(s):  
Akihiro Tanimoto ◽  
Daniel Pouliquen ◽  
Burkhard P. Kreft ◽  
David D. Stark
Keyword(s):  
Spatial Distribution ◽  
Iron Oxide ◽  
Proton Relaxation ◽  
Particulate Iron ◽  
Proton Relaxation Enhancement

Proton relaxation enhancement of albumin, immunoglobulin g, and fibrinogen labeled with gd-dtpa

1990 ◽  
Vol 13 (1) ◽  
pp. 38-43 ◽  
Author(s):  
Hannu Paajanen ◽  
Timo Reisto ◽  
Ilkka Hemmilä ◽  
Markku Komu ◽  
Pekka Niemi ◽  
...  
Keyword(s):  
Immunoglobulin G ◽  
Proton Relaxation ◽  
Proton Relaxation Enhancement

Initial assessment of magnetoferritin biokinetics and proton relaxation enhancement in rats

1995 ◽  
Vol 2 (10) ◽  
pp. 871-878 ◽  
Author(s):  
Jeff W.M. Bulte ◽  
Trevor Douglas ◽  
Stephen Mann ◽  
Josef Vymazal ◽  
Peter G. Laughlin ◽  
...  
Keyword(s):  
Initial Assessment ◽  
Proton Relaxation ◽  
Proton Relaxation Enhancement

A comparison of the proton relaxation enhancement properties of iron (III) and manganese (III) TPPS4 in solution and tissue

1986 ◽  
Vol 4 (2) ◽  
pp. 143
Author(s):  
R.J. Fiel ◽  
T.M. Button ◽  
D. Musser ◽  
S. Gilani ◽  
N. Razack ◽  
...  
Keyword(s):  
Proton Relaxation ◽  
Proton Relaxation Enhancement

The Lanthanide Cations as Probes in Biological Systems. Proton Relaxation Enhancement Studies for Model Systems and Lysozyme

1971 ◽  
Vol 21 (2) ◽  
pp. 204-209 ◽  
Author(s):  
Raymond A. Dwek ◽  
Rex E. Richards ◽  
Ken G. Morallee ◽  
Evert Nieboer ◽  
Robert J. P. Williams ◽  
...  
Keyword(s):  
Biological Systems ◽  
Model Systems ◽  
Proton Relaxation ◽  
Lanthanide Cations ◽  
Proton Relaxation Enhancement

Magnetic Resonance Studies of Concanavalin A: Conformational Changes Induced by Ca2+ and α-Methyl-D-mannopyranoside

1975 ◽  
Vol 53 (3) ◽  
pp. 371-379 ◽  
Author(s):  
Brian H. Barber ◽  
Jeremy P. Carver
Keyword(s):  
Magnetic Resonance ◽  
Concanavalin A ◽  
Metal Ion ◽  
Proton Magnetic Resonance ◽  
Structural Features ◽  
Proton Relaxation ◽  
Resonance Spectroscopy ◽  
Con A ◽  
Proton Relaxation Enhancement ◽  
Solvent Proton

Three independent solution spectroscopic techniques (solvent proton relaxation enhancement, circular dichroism, and high resolution 220 MHz proton magnetic resonance spectroscopy) have been utilized to demonstrate metal ion- and monosaccharide inhibitor-induced structural perturbations for the dimeric form of the plant lectin concanavalin A (Con A). The results indicate that (i) the occupation of the transition metal ion site S1 by Mn2+ or Zn2+ does not detectably perturb the demetallized protein conformation, (ii) the binding of Ca2+ to the Con A – Mn2+ or Con A – Zn2+ complexes perturbs the protein structure in the vicinity of the S1 site as well as at points remote from the S1–S2 double ion site, and (iii) the binding of the monosaccharide inhibitor α-methyl-D-mannopyranoside to the fully metallized Con A complex also significantly perturbs the structural features of the protein.A detailed radio frequency dependence analysis of the Ca2+ effect on the solvent proton relaxation enhancement properties of the Con A – Mn2+ complex indicates that the considerable reduction in the observed enhancement upon Ca2+ binding principally results from an approximate 120-fold decrease in the single Mn2+ water of hydration exchange rate. The 220 MHz proton magnetic resonance spectra for Con A indicate that this form of spectroscopy is the most useful of those utilized in detailing the solution structural features of this lectin, and a tentative assignment for the C-2-H proton of histidine residue 24 (the S1 site ligand) has been proposed.

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