The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Solvent denaturation
Abstract
Solvent denaturation is developed along thermodynamic lines rather than from multiple‐binding theory. Almost all the relations derivable from site‐binding theory have their counterparts in the thermodynamic formulation showing that the details of binding models may be sufficient but are not necessary for the general description of solvent denaturation. Equations are derived for the effect of denaturant concentration on stability at constant temperature and on tm. It is recommended that the thermodynamic treatment be used instead of binding models unless stoichiometric interactions are demonstrable experimentally.
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
AREAS, VOLUMES, PACKING, AND PROTEIN STRUCTURE
Richards, F. M. (1977) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.06.060177.001055 · Cited by 2,661
Structural invariants in protein folding
Chothia, C. (1975) · Nature · doi:10.1038/254304a0 · Cited by 869
Greene, R. F., & Pace, C. N. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79739-5 · Cited by 800
Introduction to Mathematical Statistics.
Doksum, K., Hogg, R. V., & Craig, A. T. (1971) · Journal of the American Statistical Association · doi:10.2307/2283566 · Cited by 790
On the Conformational Stability of Globular Proteins
von Hippel, P. H., & Wong, K.-Y. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97128-0 · Cited by 518
Light Scattering in Multi-Component Systems
STOCKMAYER, W. H. (1950) · The Journal of Chemical Physics · doi:10.1063/1.1747457 · Cited by 416
Schellman, J. A. (1975) · Biopolymers · doi:10.1002/bip.1975.360140509 · Cited by 377
Self-citationLee, J. C., & Timasheff, S. N. (1974) · Biochemistry · doi:10.1021/bi00699a005 · Cited by 333
(1957) · Nuclear Physics · doi:10.1016/0029-5582(57)90010-x · Cited by 310
Aune, K. C., & Tanford, C. (1969) · Biochemistry · doi:10.1021/bi00839a053 · Cited by 268
Cited by
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
Globular proteins at solid/liquid interfaces
Haynes, C. A., & Norde, W. (1994) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/0927-7765(94)80066-9 · Cited by 852
Factors affecting short-term and long-term stabilities of proteins
Arakawa, T., Prestrelski, S. J., Kenney, W. C., & Carpenter, J. F. (2001) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(00)00144-7 · Cited by 640
Protein interactions with urea and guanidinium chloride
Makhatadze, G. I., & Privalov, P. L. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90963-k · Cited by 623
Unfolding of Ribonuclease A on Silica Nanoparticle Surfaces
Shang, W., Nuffer, J. H., Dordick, J. S., & Siegel, R. W. (2007) · Nano Letters · doi:10.1021/nl070777r · Cited by 263
Metadata
- Authors
- Schellman, J. A.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1978-05
- Volume
- 17
- Issue
- 5
- Pages
- 1305-1322
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W4248782386
- Cited by
- 389
- References
- 14
- FWCI
- 0.90
- 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: Solvent denaturation. https://app.cochat.ai/papers/10.1002/bip.1978.360170515
- The paper
- Schellman, J. A. (1978). Solvent denaturation. Biopolymers. https://doi.org/10.1002/bip.1978.360170515
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.
