scholarly journals Nuclear magnetic resonance structure of calcium-binding protein 1 in a Ca2+ -bound closed state: Implications for target recognition

2011 ◽  
Vol 20 (8) ◽  
pp. 1356-1366 ◽  
Author(s):  
Saebomi Park ◽  
Congmin Li ◽  
James B. Ames
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Calcium Binding ◽  
Target Recognition ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Closed State ◽  
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.

Nuclear Magnetic Resonance Structure Elucidation of Peptideb2Ions

2014 ◽  
Vol 127 (5) ◽  
pp. 1567-1570 ◽  
Author(s):  
Pengyuan Liu ◽  
R. Graham Cooks ◽  
Hao Chen
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Structure Elucidation ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Nuclear Magnetic

Nuclear Magnetic Resonance Structure of a Prototype Lin12-Notch Repeat Module from Human Notch1†

Biochemistry ◽  
2003 ◽  
Vol 42 (23) ◽  
pp. 7061-7067 ◽  
Author(s):  
Didem Vardar ◽  
Christopher L. North ◽  
Cheryll Sanchez-Irizarry ◽  
Jon C. Aster ◽  
Stephen C. Blacklow
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Nuclear Magnetic

scholarly journals Nuclear Magnetic Resonance Structure and IgE Epitopes of Blo t 5, a Major Dust Mite Allergen

2008 ◽  
Vol 181 (4) ◽  
pp. 2586-2596 ◽  
Author(s):  
Siew Leong Chan ◽  
Tan Ching Ong ◽  
Yun Feng Gao ◽  
Yuen Sung Tiong ◽  
De Yun Wang ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Mite Allergen ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Dust Mite ◽  
Dust Mite Allergen ◽  
Nuclear Magnetic
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