The hydrophobic effect

By Biman Bagchi. 2013

443 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Endocrine and Autonomic Systems, Nutrition and Dietetics

View Paper: https://www.semanticscholar.org/paper/3da8c1cd2e66c47a16a18963a22e3620d5c30aeb

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. John C. Dearden
2. Daniel E. Otzen

In Endocrine and Autonomic Systems

1. John C. Dearden
2. Daniel E. Otzen

In Nutrition and Dietetics

1. John C. Dearden
2. Daniel E. Otzen

Citations in the corpus

• In silico prediction of aqueous solubility (2006, result): “Two studies in particular that appear to involve overfitting are those of Ruelle and Kesselring [86] and Yaffe et al.”
• Protein-surfactant interactions: a tale of many states. (2011, methodology): “Based on the seminal work by Reynolds and Tanford who measured intrinsic viscosities [23,76], the shape in SDS is generally depicted as a “rod-like” prolate ellipsoidal protein–surfactant aggregate.”
• Folding and assembly of β-barrel membrane proteins (2004, background): “This is only about 20% of the standard value for the hydrophobic effect [61].”