Pub. Date : 2022
PMID : 35574260
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Here, we use atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to measure the stability of protein neutrophil gelatinase-associated lipocalin (also known as NGAL, siderocalin, lipocalin 2) that can bind iron through the cation-pi interactions between its three cationic residues and the iron-binding tri-catechols. | Iron | lipocalin 2 | Homo sapiens |
| 2 | Here, we use atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to measure the stability of protein neutrophil gelatinase-associated lipocalin (also known as NGAL, siderocalin, lipocalin 2) that can bind iron through the cation-pi interactions between its three cationic residues and the iron-binding tri-catechols. | Iron | lipocalin 2 | Homo sapiens |
| 3 | Here, we use atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to measure the stability of protein neutrophil gelatinase-associated lipocalin (also known as NGAL, siderocalin, lipocalin 2) that can bind iron through the cation-pi interactions between its three cationic residues and the iron-binding tri-catechols. | Iron | lipocalin 2 | Homo sapiens |
| 4 | Here, we use atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to measure the stability of protein neutrophil gelatinase-associated lipocalin (also known as NGAL, siderocalin, lipocalin 2) that can bind iron through the cation-pi interactions between its three cationic residues and the iron-binding tri-catechols. | Iron | lipocalin 2 | Homo sapiens |
| 5 | Then, the same NGAL but bound with the iron-catechol complexes through the cation-pi interactions as a holo-form was characterized. | Iron | lipocalin 2 | Homo sapiens |