The osmophobic effect: natural selection of a thermodynamic force in protein folding.

By D. Bolen, I. Baskakov. Journal of Molecular Biology, 2001

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Industrial Production of the Cell Protectant Ectoine: Protection Mechanisms, Processes, and Products (2014, background): “The work of the Bolen group has identified the peptide backbone as the major player for binding/repulsion effects, and subsequent protein stabilization [37, 38] and named this phenomenon the osmophobic effect [39].”
Diversity, distribution and roles of osmoprotective compounds accumulated in halophytes under abiotic stress. (2015, background): “Termed the ‘osmophobic’ effect by Bolen and Baskakov (2001), exclusion arises from an apparent repulsion between stabilizers and the peptide backbone, explaining how this effect can be universal.”
Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses (2005, background): “Recently termed the ‘osmophobic’ effect by Bolen and Baskakov (2001), exclusion arises from an apparent repulsion between stabilizers and the peptide backbone, explaining how this effect can be universal.”
Assessing protein disorder and induced folding (2005, background): “providing an additional force for folding that has no preference for any particular secondary structure.(219) Based on the molecular origin of TMAO-driven protein folding, if”
Proline Mechanisms of Stress Survival (2013, background): “Relative to other osmolytes, proline is categorized as a weak stabilizer of protein folding and ranks lower in ability to induce protein folding (7, 11).”