Temperature dependence of hydrophobic interactions: A mean force perspective

By S. Shimizu, Hue Sun Chan. 2000

149 citations recorded by the source corpus.

Subfields: Atomic and Molecular Physics, and Optics, Fluid Flow and Transfer Processes, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/ec8adc0587b356a584c9634f6d852975467a1d03

How researchers see this paper

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

In Atomic and Molecular Physics, and Optics

1. José N. Onuchic

In Molecular Biology

1. Ryan R. Cheng
2. Faruck Morcos
3. José N. Onuchic
4. Martin Weigt
5. Anne-Florence Bitbol
6. Sergey Ovchinnikov
7. Debora Marks
8. Ned S. Wingreen

Citations in the corpus

• Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection (2014, methodology): “The physical model used in this study assumes that the effective interactions between amino acid residues are temperature-independent, an approximation that breaks down because of solvent effects (24).”