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Cited by 1,048

The DOI matches its Crossref record; 132 of the 132 references it cites were found in a registry or an index.

WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION

Levy, Yaakov, Onuchic, José N.·2006·Annual Review of Biophysics and Biomolecular Structure

Abstract

Water is essential for life in many ways, and without it biomolecules might no longer truly be biomolecules. In particular, water is important to the structure, stability, dynamics, and function of biological macromolecules. In protein folding, water mediates the collapse of the chain and the search for the native topology through a funneled energy landscape. Water actively participates in molecular recognition by mediating the interactions between binding partners and contributes to either enthalpic or entropic stabilization. Accordingly, water must be included in recognition and structure prediction codes to capture specificity. Thus water should not be treated as an inert environment, but rather as an integral and active component of biomolecular systems, where it has both dynamic and structural roles. Focusing on water sheds light on the physics and function of biological machinery and self-assembly and may advance our understanding of the natural design of proteins and nucleic acids.

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Crossref · 10.1146/annurev.biophys.35.040405.102134

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Metadata

Authors
Levy, Y., & Onuchic, J. N.
Venue
Annual Review of Biophysics and Biomolecular Structure
Published
2006-06-01
Volume
35
Issue
1
Pages
389-415
ISSN
  • 1056-8700 (ISSN-L)
  • 1545-4266
OpenAlex
W2104529244
Cited by
1,048
References
132
FWCI
15.47
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION. https://app.cochat.ai/papers/10.1146/annurev.biophys.35.040405.102134
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Levy, Y., & Onuchic, J. N. (2006). WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.35.040405.102134

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