๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Structure and thermodynamics of RNA-protein binding: using molecular dynamics and free energy analyses to calculate the free energies of binding and conformational change

โœ Scribed by Carolina M. Reyes; Peter A. Kollman

Book ID
115630123
Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
612 KB
Volume
297
Category
Article
ISSN
0022-2836

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

Free energy perturbation and molecular d
Free energy perturbation and molecular dynamics calculations of copper binding to azurin
โœ Matteo Pappalardo; Danilo Milardi; Domenico M. Grasso; Carmelo La Rosa ๐Ÿ“‚ Article ๐Ÿ“… 2003 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 184 KB

## Abstract Free energy perturbation/molecular dynamics simulations have been carried out on copper/azurin systems calculating the binding affinities of copper (II) ion to azurin either in the native or in the unfolded state. In order to test the validity of the strategy adopted for the calculation

Conformation of the Ras-binding domain o
Conformation of the Ras-binding domain of Raf studied by molecular dynamics and free energy simulations
โœ Jun Zeng; Herbert R. Treutlein; Thomas Simonson ๐Ÿ“‚ Article ๐Ÿ“… 1998 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 693 KB

Recognition of Ras by its downstream target Raf is mediated by a Rasrecognition region in the Ras-binding domain (RBD) of Raf. Residues 78-89 in this region occupy two different conformations in the ensemble of NMR solution structures of the RBD: a fully โฃ-helical one, and one where 87-90 form a typ