Articolele autorului Vlad Cojocaru
Link la profilul stiintific al lui Vlad Cojocaru

Loss of G-A base pairs is insufficient for achieving a large opening of U4 snRNA K-turn motif

Upon binding to the 15.5K protein, two tandem-sheared G–A base pairs are formed in the internal loop of the kink-turn motif of U4 snRNA (Kt-U4). We have reported that the folding of Kt-U4 is assisted by protein binding. Unstable interactions that contribute to a large opening of the free RNA (‘k–e motion’) were identified using locally enhanced sampling molecular dynamics simulations, results that agree with experiments. A detailed analysis

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Molecular motions at the 5′ stem-loop of U4 snRNA: Implications for U4/U6 snRNP assembly
Primordial germ cell migration in the chick and mouse embryo: the role of the chemokine SDF-1/CXCL12
The snRNP 15.5K protein folds its cognate K-turn RNA. A combined theoretical and biochemical study

The human 15.5K protein binds to the 5' stem–loop of U4 snRNA, promotes the assembly of the spliceosomal U4/U6 snRNP, and is required for the recruitment of the 61K protein and the 20/60/90K protein complex to the U4 snRNA. In the crystallographic structure of the 15.5K–U4 snRNA complex, the conformation of the RNA corresponds to the family of kink-turn (K-turn) structural motifs. We simulated the complex and the free RNA, showing how the protein

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