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

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书目名称Biomolecular Structure and Dynamics影响因子(影响力)




书目名称Biomolecular Structure and Dynamics影响因子(影响力)学科排名




书目名称Biomolecular Structure and Dynamics网络公开度




书目名称Biomolecular Structure and Dynamics网络公开度学科排名




书目名称Biomolecular Structure and Dynamics被引频次




书目名称Biomolecular Structure and Dynamics被引频次学科排名




书目名称Biomolecular Structure and Dynamics年度引用




书目名称Biomolecular Structure and Dynamics年度引用学科排名




书目名称Biomolecular Structure and Dynamics读者反馈




书目名称Biomolecular Structure and Dynamics读者反馈学科排名

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Approaches to Protein-Ligand Binding from Computer Simulationsations of statistical mechanics simulations to the problem are considered that feature full atomic-level descriptions of the protein, ligand and aqueous environment. Basic concepts on the methodology and intermolecular interactions in solution are presented along with results of Monte Carlo simulati

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Dynamics of Biomolecules : Simulation Versus X-Ray and Far-Infrared Experimentsular mobility [1]. In many areas of molecular biology, such as muscle contraction or conformational changes in allosteric proteins, motion is self-evidently crucial. In facilitating such processes as the access of ligands to protein binding sites or in accomodating the change in protein and substrat

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Professional Gamblingortance for the design of drugs. Structural information often greatly enhances our understanding of how proteins function and how they interact with each other or it can, for example, explain antigenic behaviour, DNA binding specificity, etc. X-ray crystallography and NMR spectroscopy are the only w

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Biomolecular Structure and Dynamics: Recent Experimental and Theoretical Advances study of biomolecules in solution, thus closer to their real physiological environment. The method is limited, however, to biomolecules of relatively small size due to limitations in spectral resolution and line broadening effects. The upper limit is presently situated around molecular weights of 3

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What Drives Association of α-Helical Peptides in Membrane Domains of Proteins? Role of Hydrophobic Ipore-forming proteins. Their hydrophobic and packing properties were analyzed using Monte Carlo simulations in solvents of different polarity, molecular hydrophobicity potential calculations and environmental profiles method. The results obtained in independent techniques are in reasonable agreement

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