Proton nuclear magnetic resonance studies of the interaction of the lanthanide ions ytterbium and lutetium with apo- and calcium-saturated porcine intestinal calcium binding protein

Biochemistry ◽  
1985 ◽  
Vol 24 (9) ◽  
pp. 2332-2338 ◽  
Author(s):  
Judith G. Shelling ◽  
Theo Hofmann ◽  
Brian D. Sykes
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Lanthanide Ions ◽  
Proton Nuclear Magnetic Resonance ◽  
Magnetic Resonance Studies ◽  
Nuclear Magnetic

Proton nuclear magnetic resonance studies of porcine intestinal calcium binding protein

Biochemistry ◽  
1983 ◽  
Vol 22 (11) ◽  
pp. 2649-2654 ◽  
Author(s):  
Judith G. Shelling ◽  
Brian D. Sykes ◽  
Joseph D. J. O'Neil ◽  
Theo Hofmann
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Proton Nuclear Magnetic Resonance ◽  
Magnetic Resonance Studies ◽  
Nuclear Magnetic

1H nuclear magnetic resonance studies of ytterbium-substituted porcine intestinal calcium-binding protein

1985 ◽  
Vol 63 (9) ◽  
pp. 992-997 ◽  
Author(s):  
Judith G. Shelling ◽  
Theo Hofmann ◽  
Brian D. Sykes
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Binding ◽  
Calcium Binding ◽  
Chemical Exchange ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Line Broadening ◽  
1H Nuclear Magnetic Resonance ◽  
Nuclear Magnetic

The addition of ytterbium to calcium-saturated porcine intestinal calcium-binding protein resulted in the appearance of broad lanthanide-shifted resonances well outside the normally observed region of the 1H nuclear magnetic resonance spectrum of the calcium form of the protein. Variation of the salt concentration and temperature have led us to conclude that aggregation and chemical exchange do not contribute to the line widths of these resonances. Assuming that the line broadening of these lanthanide-shifted resonances arises from the contribution of the susceptibility line-broadening mechanism for protein residues proximal to the bound Yb3+ ion, we have calculated Yb3+–proton distances for nuclei in the metal-binding site. These lanthanide-shifted resonances provide very sensitive probes of the structure of the protein in solution.

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