The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The Role of Solvent Viscosity in the Dynamics of Protein Conformational Changes
Abstract
Nanosecond lasers were used to measure the rate of conformational changes in myoglobin after ligand dissociation at ambient temperatures. At low solvent viscosities the rate is independent of viscosity, but at high viscosities it depends on approximately the inverse first power of the viscosity. Kramers theory for unimolecular rate processes can be used to explain this result if the friction term is modified to include protein as well as solvent friction. The theory and experiment suggest that the dominant factor in markedly reducing the rate of conformational changes in myoglobin at low temperatures (<200 K) is the very high viscosity (>10 7 centipoise) of the glycerol-water solvent. That is, at low temperatures conformational substates may not be "frozen" so much as "stuck."
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
Reaction-rate theory: fifty years after Kramers
Hänggi, P., Talkner, P., & Borkovec, M. (1990) · Reviews of Modern Physics · doi:10.1103/revmodphys.62.251 · Cited by 6,154
Cited by
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
WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION
Levy, Y., & Onuchic, J. N. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102134 · Cited by 1,048
Protein folding in the landscape perspective: Chevron plots and non-arrhenius kinetics
Chan, H. S., & Dill, K. A. (1998) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19980101)30:1<2::aid-prot2>3.0.co;2-r · Cited by 438
Direct observation of fast protein folding: the initial collapse of apomyoglobin.
Ballew, R. M., Sabelko, J., & Gruebele, M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5759 · Cited by 314
Fast events in protein folding initiated by nanosecond laser photolysis.
Jones, C. M., Henry, E. R., Hu, Y., Chan, C. K., Luck, S. D., Bhuyan, A., Roder, H., Hofrichter, J., & Eaton, W. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.24.11860 · Cited by 306
Self-citation
Metadata
- Authors
- Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., & Eaton, W. A.
- Venue
- Science
- Published
- 1992-06-26
- Volume
- 256
- Issue
- 5065
- Pages
- 1796-1798
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1981716245
- Cited by
- 550
- References
- 1
- FWCI
- 4.45
- 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: The Role of Solvent Viscosity in the Dynamics of Protein Conformational Changes. https://app.cochat.ai/papers/10.1126/science.1615323
- The paper
- Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., & Eaton, W. A. (1992). The Role of Solvent Viscosity in the Dynamics of Protein Conformational Changes. Science. https://doi.org/10.1126/science.1615323
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.
