Pub. Date : 1997 Dec 1
PMID : 9390185
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Here, we study the accessibility of the fluorescein covalently attached to the Lys515 at the nucleotide binding domain of the ATPase to the small collisional quencher iodide at pH 6 and 8, as well as the effect of ligand binding (La3+, La(3+)-nucleotide, and Ca2+). | Fluorescein | dynein axonemal heavy chain 8 | Homo sapiens |
| 2 | Our results indicate that bound fluorescein is significantly more accessible at pH 6 than at pH 8, suggesting that pH modulates the structure of the nucleotide binding domain of the ATPase. | Fluorescein | dynein axonemal heavy chain 8 | Homo sapiens |
| 3 | Notably, the differential accessibility of the nucleotide binding domain at acidic and basic pH cannot be rationalized in terms of the ATPase E1/E2 conformational equilibrium since a shift of the ATPase toward the E1 (plus Ca2+) or E2 (plus EGTA) did not affect the accessibility of fluorescein-labeled ATPase to the quencher. | Fluorescein | dynein axonemal heavy chain 8 | Homo sapiens |
| 4 | Notably, the differential accessibility of the nucleotide binding domain at acidic and basic pH cannot be rationalized in terms of the ATPase E1/E2 conformational equilibrium since a shift of the ATPase toward the E1 (plus Ca2+) or E2 (plus EGTA) did not affect the accessibility of fluorescein-labeled ATPase to the quencher. | Fluorescein | dynein axonemal heavy chain 8 | Homo sapiens |