The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Thermodynamic and kinetic examination of protein stabilization by glycerol
Abstract
The effect of concentrated glycerol on the thermal transitions of chymotrypsinogen and ribonuclease has been examined by differential spectrophotometry at 293 and 287 mm, respectively. It was found that for both proteins addition of glycerol raises the transition temperature, the increase in Tm being greater for ribonuclease than for chymotrypsinogen. This increase in the free energy of denaturation appears to reflect primarily a decrease in the entropy change. Analysis in terms of the Wyman linkage equation shows that, for both proteins, the exclusion of glycerol from the protein domain increases on denaturation i.e., the chemical potential of glycerol becomes even more positive when the protein unfolds relative to the native structure. This provides the thermodynamic stabilization free energy. Results of the kinetic examination of the slow unfolding reaction are consistent with the concept that the preferential exclusion of glycerol is related, at least in part, to enhanced solvent ordering.
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
Protein denaturation. C. Theoretical models for the mechanism of denaturation.
Tanford, C. (1970) · PubMed · Cited by 1,546
Brandts, J. F., Halvorson, H. R., & Brennan, M. (1975) · Biochemistry · doi:10.1021/bi00693a026 · Cited by 1,113
Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of Proteins
Tanford, C. (1962) · Journal of the American Chemical Society · doi:10.1021/ja00881a009 · Cited by 1,005
Némethy, G., & Scheraga, H. A. (1962) · The Journal of Physical Chemistry · doi:10.1021/j100816a004 · Cited by 973
On the average hydrophobicity of proteins and the relation between it and protein structure
Bigelow, C. C. (1967) · Journal of Theoretical Biology · doi:10.1016/0022-5193(67)90004-5 · Cited by 793
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
Brandts, J. F., & Hunt, L. (1967) · Journal of the American Chemical Society · doi:10.1021/ja00995a002 · Cited by 425
Robinson, D. R., & Jencks, W. P. (1965) · Journal of the American Chemical Society · doi:10.1021/ja01089a028 · Cited by 423
Lee, J. C., & Timasheff, S. N. (1974) · Biochemistry · doi:10.1021/bi00699a005 · Cited by 333
Self-citationIn vitro reconstitution of calf brain microtubules: effects of solution variables
Lee, J. C., & Timasheff, S. N. (1977) · Biochemistry · doi:10.1021/bi00627a037 · Cited by 332
Self-citationTsong, T. Y., Hearn, R. P., Wrathall, D. P., & Sturtevant, J. M. (1970) · Biochemistry · doi:10.1021/bi00815a015 · Cited by 243
Brandts, J. F. (1964) · Journal of the American Chemical Society · doi:10.1021/ja01074a014 · Cited by 216
Thermodynamic investigations of proteins
Pfeil, W., & Privalov, P. L. (1976) · Biophysical Chemistry · doi:10.1016/0301-4622(76)80004-x · Cited by 199
Gerlsma, S. Y. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93609-4 · Cited by 158
Cis‐Trans equilibrium and kinetic studies of acetyl‐ L ‐proline and glycyl‐ L ‐proline
Cheng, H. N., & BOVEY, F. A. (1977) · Biopolymers · doi:10.1002/bip.1977.360160707 · Cited by 145
Kinetic Evidence for Incorrectly Folded Intermediate States in the Refolding of Denatured Proteins
Ikai, A., & Tanford, C. (1971) · Nature · doi:10.1038/230100a0 · Cited by 133
Cited by
The stabilization of proteins by osmolytes
Arakawa, T., & Timasheff, S. N. (1985) · Biophysical Journal · doi:10.1016/s0006-3495(85)83932-1 · Cited by 1,020
Self-citationImproved vitrification solutions based on the predictability of vitrification solution toxicity
Fahy, G. M., Wowk, B., Wu, J., & Paynter, S. (2004) · Cryobiology · doi:10.1016/j.cryobiol.2003.11.004 · Cited by 284
Correcting temperature-sensitive protein folding defects
Brown, C. R., Hong-Brown, L. Q., & Welch, W. J. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119302 · Cited by 176
How to prevent losses of protein by adsorption to glass and plastic
Suelter, C. H., & DeLuca, M. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90738-8 · Cited by 105
Structural insights into adeno-associated virus serotype 5
Govindasamy, L., DiMattia, M. A., Gurda, B. L., Halder, S., McKenna, R., Chiorini, J. A., Muzyczka, N., Zolotukhin, S., & Agbandje-McKenna, M. (2013) · Journal of Virology · doi:10.1128/jvi.00867-13 · Cited by 95
Metadata
- Authors
- Gekko, K., & Timasheff, S. N.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1981-08-01
- Volume
- 20
- Issue
- 16
- Pages
- 4677-4686
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2014896559
- Cited by
- 481
- References
- 17
- FWCI
- 5.25
- 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
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.
