Pub. Date : 2014 Dec
PMID : 25137638
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The conserved turn structure at Val24-Lys28 in all peptides and Zn2+-bound Abeta42 is confirmed as the common structural motif to nucleate folding of Abeta. | Zinc | amyloid beta precursor protein | Homo sapiens |
| 2 | We characterize the different populations of correlated domain motions for each mutant from a more macroscopic perspective, and unexpectedly find that Zn2+-bound Abeta42 ensemble shares the same populations as Abeta42, indicating that the binding of Zn2+ to Abeta follows the conformational selection mechanism, and thus is independent of domain motions, even though the structures of Abeta have been modified at a residue level. | Zinc | amyloid beta precursor protein | Homo sapiens |
| 3 | We characterize the different populations of correlated domain motions for each mutant from a more macroscopic perspective, and unexpectedly find that Zn2+-bound Abeta42 ensemble shares the same populations as Abeta42, indicating that the binding of Zn2+ to Abeta follows the conformational selection mechanism, and thus is independent of domain motions, even though the structures of Abeta have been modified at a residue level. | Zinc | amyloid beta precursor protein | Homo sapiens |
| 4 | We characterize the different populations of correlated domain motions for each mutant from a more macroscopic perspective, and unexpectedly find that Zn2+-bound Abeta42 ensemble shares the same populations as Abeta42, indicating that the binding of Zn2+ to Abeta follows the conformational selection mechanism, and thus is independent of domain motions, even though the structures of Abeta have been modified at a residue level. | Zinc | amyloid beta precursor protein | Homo sapiens |