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
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Some Factors in the Interpretation of Protein Denaturation
Kauzmann, W. (1959) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60608-7 · Cited by 4,870
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,800
Interfaces and the driving force of hydrophobic assembly
Chandler, D. (2005) · Nature · doi:10.1038/nature04162 · Cited by 3,591
Agmon, N. (1995) · Chemical Physics Letters · doi:10.1016/0009-2614(95)00905-j · Cited by 3,482
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648 · cited 1×
“TSE: transition state ensemble ability to efficiently organize the polypeptide chain into a specific structure (16, 86, 105, 106).”
BackgroundSelf-citation[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
Pace, C. N. (1986) · Methods in Enzymology · doi:10.1016/0076-6879(86)31045-0 · Cited by 2,258
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Self-citationImproving enzymes by using them in organic solvents
Klibanov, A. M. (2001) · Nature · doi:10.1038/35051719 · Cited by 2,152
Anatomy of hot spots in protein interfaces
Bogan, A. A., & Thorn, K. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1843 · Cited by 1,988
Cited by
Water Dynamics in the Hydration Shells of Biomolecules
Laage, D., Elsaesser, T., & Hynes, J. T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00765 · Cited by 913
On the Molecular Mechanism of Water Reorientation
Laage, D., & Hynes, J. T. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp805217u · Cited by 438
Guedes, I. A., Pereira, F. S. S., & Dardenne, L. E. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01089 · Cited by 331
Martin-Jimenez, D., Chacon, E., Tarazona, P., & Garcia, R. (2016) · Nature Communications · doi:10.1038/ncomms12164 · Cited by 198
Energy landscape in protein folding and unfolding
Mallamace, F., Corsaro, C., Mallamace, D., Vasi, S., Vasi, C., Baglioni, P., Buldyrev, S. V., Chen, S.-H., & Stanley, H. E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1524864113 · Cited by 122
Metadata
- Authors
- Levy, Y., & Onuchic, J. N.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION. https://app.cochat.ai/papers/10.1146/annurev.biophys.35.040405.102134
- The paper
- 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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.