The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Protein dynamics
Abstract
The biological activity of protein molecules depends on their structural fluctuations. Recent theoretical studies have helped to clarify the nature and function of these fluctuations. Because proteins are large densely-packed structures their atomic motions can be compared to those that occur in other dense materials. Small motions at short times are similar to what is observed in liquids. Larger motions in proteins are opposed by the forces that stabilise their native structures, resulting in solid-like features. Of special importance is the strong coupling observed between local and collective displacements; this coupling governs the character of many ligand-binding processes and structural transformations that are essential to biological function.
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
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
Cited by
Ultrafast excitation energy transfer dynamics in photosynthetic pigment–protein complexes
Renger, T., May, V., & Kühn, O. (2001) · Physics Reports · doi:10.1016/s0370-1573(00)00078-8 · Cited by 413
Computational statistical mechanics methodology, applications and supercomputing
Abraham, F. F. (1986) · Advances in Physics · doi:10.1080/00018738600101851 · Cited by 306
Protein generation with evolutionary diffusion: sequence is all you need
Alamdari, S., Thakkar, N., van den Berg, R., Tenenholtz, N., Strome, R., Moses, A. M., Lu, A. X., Fusi, N., Amini, A. P., & Yang, K. K. (2023) · doi:10.1101/2023.09.11.556673 · Cited by 154
Okamoto, C., & Ando, K. (2024) · Biophysics and Physicobiology · doi:10.2142/biophysico.bppb-v21.0007 · Cited by 19
Metadata
- Authors
- McCammon, J. A.
- Venue
- Reports on Progress in Physics
- Publisher
- IOP Publishing
- Published
- 1984-01-01
- Volume
- 47
- Issue
- 1
- Pages
- 1-46
- ISSN
- 0034-4885 (ISSN-L)
- 1361-6633
- OpenAlex
- W3088604011
- Cited by
- 270
- References
- 1
- FWCI
- 6.74
- 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: Protein dynamics. https://app.cochat.ai/papers/10.1088/0034-4885/47/1/001
- The paper
- McCammon, J. A. (1984). Protein dynamics. Reports on Progress in Physics. https://doi.org/10.1088/0034-4885/47/1/001
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.
