The DOI matches its Crossref record.
A consistent picture of protein dynamics.
Open accessAbstract
Information about the protein dynamics of myoglobin obtained by x-ray and Mössbauer investigations is analyzed and compared with computer simulations. Computer simulations give correct amplitudes of mean-square displacements but fail in the description of the time dependence of motions. Our model describes protein dynamics at physiological temperatures as an overdamped diffusion-like motion in a restricted space. The fluctuations occur around the average conformation determined by x-ray structure analysis. The gain in entropy drives the molecule into the transition state and, in this way, accounts for its flexibility.
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
Cited by
Protein states and proteinquakes.
Ansari, A., Berendzen, J., Bowne, S. F., Frauenfelder, H., Iben, I. E., Sauke, T. B., Shyamsunder, E., & Young, R. D. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.15.5000 · Cited by 828
Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Young, R. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405573101 · Cited by 524
Clore, G. M., Driscoll, P. C., Wingfield, P. T., & Gronenborn, A. M. (1990) · Biochemistry · doi:10.1021/bi00484a006 · Cited by 437
Thomas, D. J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80892-k · Cited by 15
Hydration of Intrinsically Disordered Proteins from Wide‐Line NMR
Tompa, K., Bokor, M., & Tompa, P. (2010) · Instrumental Analysis of Intrinsically Disordered Proteins · doi:10.1002/9780470602614.ch12 · Cited by 8
Metadata
- Authors
- Parak, F., & Knapp, E. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1984-11
- Volume
- 81
- Issue
- 22
- Pages
- 7088-7092
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2055038996
- Cited by
- 158
- References
- 0
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- bronze
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: A consistent picture of protein dynamics. https://app.cochat.ai/papers/10.1073/pnas.81.22.7088
- The paper
- Parak, F., & Knapp, E. W. (1984). A consistent picture of protein dynamics. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.81.22.7088
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.