Circularly polarized luminescence from terbium(III) as a probe of metal ion binding in calcium-binding proteins

Biochemistry ◽  
1992 ◽  
Vol 31 (34) ◽  
pp. 7970-7976 ◽  
Author(s):  
Nursen Coruh ◽  
James P. Riehl
Keyword(s):  
Calcium Binding ◽  
Metal Ion ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Circularly Polarized ◽  
Circularly Polarized Luminescence ◽  
Polarized Luminescence

Locating the Metal Ion in Calcium-Binding Proteins by Using Cerium(III) as a Probe

ChemBioChem ◽  
2001 ◽  
Vol 2 (7-8) ◽  
pp. 550-558 ◽  
Author(s):  
Ivano Bertini ◽  
Yong-Min Lee ◽  
Claudio Luchinat ◽  
Mario Piccioli ◽  
Luisa Poggi
Keyword(s):  
Calcium Binding ◽  
Metal Ion ◽  
Binding Proteins ◽  
Calcium Binding Proteins

GLOBAL METAL-ION BINDING PROTEIN FINGERPRINT: A METHOD TO IDENTIFY MOTIF-LESS METAL-ION BINDING PROTEINS

2010 ◽  
Vol 08 (04) ◽  
pp. 717-726 ◽  
Author(s):  
ABHILASH MOHAN ◽  
SHARMILA ANISHETTY ◽  
PENNATHUR GAUTAM
Keyword(s):  
Metal Ion ◽  
Binding Proteins ◽  
Binding Protein ◽  
Vital Role ◽  
Ion Binding ◽  
Binding Motif ◽  
Specific Class ◽  
Metal Ion Binding ◽  
Knowledge Based ◽  
Supervised Classifiers

Metal-ion binding proteins play a vital role in biological processes. Identifying putative metal-ion binding proteins is through knowledge-based methods. These involve the identification of specific motifs that characterize a specific class of metal-ion binding protein. Metal-ion binding motifs have been identified for the common metal ions. A robust global fingerprint that is useful in identifying a metal-ion binding protein from a non-metal-ion binding protein has not been devised. Such a method will help in identifying novel metal-ion binding proteins and proteins that do not possess a canonical metal-ion binding motif. We have used a set of physico-chemical parameters of metal-ion binding proteins encoded by the genes CzcA, CzcB and CzcD as a training set to supervised classifiers and have been able to identify several other metal ion binding proteins leading us to believe that metal-ion binding proteins have a global fingerprint, which cannot be pinned down to a single feature of the protein sequence.

Quadrupolar metal ion NMR studies of metalloproteins

1998 ◽  
Vol 76 (2-3) ◽  
pp. 210-222 ◽  
Author(s):  
James M Aramini ◽  
Hans J Vogel
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Metal Ion ◽  
Chemical Information ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Nmr Studies ◽  
Small Proteins ◽  
Ion Binding Sites ◽  
Metal Ion Binding Sites

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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