Pub. Date : 1996 Jul 9
PMID : 8688416
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Structural influence of cation binding to recombinant human brain S100b: evidence for calcium-induced exposure of a hydrophobic surface. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 2 | The dimeric calcium-binding protein S100b is proposed to undergo a calcium-induced structural change allowing it to interact, via a hydrophobic surface, with other proteins. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 3 | The dimeric calcium-binding protein S100b is proposed to undergo a calcium-induced structural change allowing it to interact, via a hydrophobic surface, with other proteins. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 4 | Previously it has been suggested that calcium binding to S100b leads to the exposure of at least one phenylalanine residue (Mani et al., 1982, 1983). | Calcium | S100 calcium binding protein B | Homo sapiens |
| 5 | To study these effects, we monitored calcium binding to recombinant human S100b by NMR spectroscopy under different salt (KCI) conditions. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 6 | 15N-Labeled glycine residues in S100b showed calcium-induced chemical shift changes similar to those reported for the related monomeric protein calbindin D9k, suggesting similar conformational changes are occurring in the calcium-binding loops of these two proteins. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 7 | 15N-Labeled glycine residues in S100b showed calcium-induced chemical shift changes similar to those reported for the related monomeric protein calbindin D9k, suggesting similar conformational changes are occurring in the calcium-binding loops of these two proteins. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 8 | Calcium binding to S100b also resulted in a shifting and broadening of several 1H resonances from the Ca-S100b form only including those from the side chains of residues F14, F70, and F73 but not those of residue Y17. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 9 | Calcium binding to S100b also resulted in a shifting and broadening of several 1H resonances from the Ca-S100b form only including those from the side chains of residues F14, F70, and F73 but not those of residue Y17. | Calcium | S100 calcium binding protein B | Homo sapiens |
| 10 | These observations are consistent with the calcium-induced exposure of at least one of these hydrophobic residues, resulting in self-association of the S100b dimer. | Calcium | S100 calcium binding protein B | Homo sapiens |