A Computational Study of Procyanidin Binding to Histatin 5 and Thermodynamic Properties of Hofmeister-Anion Binding to a Hydrophobic Cavitand
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Summary
This dissertation will present the following two studies: A Computational Study of Procyanidin Binding to Histatin 5 and Thermodynamic Properties of Hofmeister-Anion Binding to a Hydrophobic Cavitand.
- Type
- article
- Published
- 2014-01-01
- Cited by
- 0
- References
- 77
- Access
- Open access
- OpenAlex
- https://openalex.org/W31254586
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:91718657
Keywords
Cavitand, Chemistry, Hofmeister series, Computational chemistry, Crystallography
References
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- Statistical Mechanics of Fluid Mixtures
- Well-defined, organic nanoenvironments in water: the hydrophobic effect drives a capsular assembly.
- Charge density-dependent strength of hydration and biological structure.
- A Comparison of Alternative Approaches to Free Energy Calculations
- M3+ Lanthanide Cation Solvation by Acetonitrile: The Role of Cation Size, Counterions, and Polarization Effects Investigated by Molecular Dynamics and Quantum Mechanical Simulations
- Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the major urinary protein.
- Cavitands: Organic Hosts with Enforced Cavities
- Enhancing the accuracy, the efficiency and the scope of free energy simulations.
- ‘Zur Lehre von der Wirkung der Salze’ (about the science of the effect of salts): Franz Hofmeister's historical papers
- A View of the Hydrophobic Effect
- Effect of ions on the structure of water: structure making and breaking.
- Anion Binding to Hydrophobic Concavity is Central to the Salting-in Effects of Hofmeister Chaotropes
- Solvent effects in molecular recognition
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