Titlebook: Biomolecular Structure and Dynamics; Gérard Vergoten,Theophile Theophanides Book 1997 Springer Science+Business Media Dordrecht 1997 Pepti

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https://doi.org/10.1007/978-3-658-24360-9ays to obtain detailed structural information. Unfortunately, these techniques involve elaborate technical procedures and many proteins fail to crystallize at all and/or cannot be obtained or dissolved in large enough quantities for NMR measurements. The size of the protein is also a limiting factor for NMR.

媽媽不開心

Sergio Herrero-Lopez,John R. Williamsck methods. The speed of the computations and the reliability of the results allow us to suggest the density functional methods as tools for the study of large and complex systems such as the biologival molecules.

廚師

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0168-132X d stochastic dynamic simulations, X-raycrystallography and NMR of biomolecules, the structure of proteins andits prediction, time resolved Fourier transform IR spectroscopy ofbiomolecules, the computation of free energy, applications ofvibrational CD of nucleic acids, and solid state NMR. Furtherpre

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不成比例

Approaches to Protein-Ligand Binding from Computer Simulationsus environment. Basic concepts on the methodology and intermolecular interactions in solution are presented along with results of Monte Carlo simulations for binding of inhibitors by trypsin and thrombin.

極端的正確性

Dynamics of Biomolecules : Simulation Versus X-Ray and Far-Infrared Experimentsdently crucial. In facilitating such processes as the access of ligands to protein binding sites or in accomodating the change in protein and substrate ge-ometries associated with an enzyme reaction, molecular motion is required.

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