1H FT NMR STUDIES OF THE Co3+-SUBSTITUTED HEXAMER: CHARACTERIZATION OF METAL ION BINDING TO THE GLU(B13) SITE

Author(s):  
Melinda Roy ◽  
Robert Lee ◽  
Michael F. Dunn
2000 ◽  
Vol 79 (1-4) ◽  
pp. 365-370 ◽  
Author(s):  
Jonathan P Hannan ◽  
Sara B.-M Whittaker ◽  
Andrew M Hemmings ◽  
Richard James ◽  
Colin Kleanthous ◽  
...  

1998 ◽  
Vol 76 (2-3) ◽  
pp. 210-222 ◽  
Author(s):  
James M Aramini ◽  
Hans J Vogel

We present a summary of the quadrupolar metal ion NMR studies of metalloproteins conducted in our laboratory in recent years. The approaches we employ can be subdivided into two categories: (i) the use of low-frequency metal nuclei to probe metal ion binding sites in small proteins, exemplified by 43Ca NMR studies of alpha-lactalbumins and calcium-binding lysozymes, and (ii) the novel detection of the central transition of half-integer quadrupolar nuclei of moderate frequency bound to large metalloproteins, typified by 27Al, 45Sc, 69,71Ga, and 51V NMR studies of the transferrins. We highlight the chemical information regarding the nature of metal ion binding sites that can be obtained from this technique and emphasize the salient parameters that an investigator must consider to successfully apply quadrupolar NMR to the study of biological macromolecules.Key words: quadrupolar NMR, metalloproteins, transferrins.


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