The DOI matches its Crossref record.
Mechanism of tertiary structural change in hemoglobin.
Open accessAbstract
A reaction path is presented by which the effects of oxygen binding in hemoglobin are transmitted from a heme group to the surface of its subunit. Starting from the known deoxy geometry, it is shown by calculations with empirical energy functions and comparisons with available data how the change in heme geometry on ligation introduces a perturbation that leads to the tertiary structural alterations essential for cooperatively. It is found that there is little strain on the unliganded heme; instead, the reduced oxygen affinity of hemoglobin results from the strain on the liganded subunit in a tetramer with the deoxy quarternary structure.
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
McCammon, J. A., Gelin, B. R., & Karplus, M. (1977) · Nature · doi:10.1038/267585a0 · Cited by 2,067
Self-citationEnergetics of enzyme catalysis.
Warshel, A. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.11.5250 · Cited by 485
Zinc binding in proteins and solution: A simple but accurate nonbonded representation
Stote, R. H., & Karplus, M. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340230104 · Cited by 354
Self-citationGurd, F. R. N., & Rothges, T. M. (1979) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60459-3 · Cited by 280
Iron: Essential for Almost All Life
Crichton, R. R. (2008) · Biological Inorganic Chemistry · doi:10.1016/b978-044452740-0.50013-2 · Cited by 10
Metadata
- Authors
- Gelin, B. R., & Karplus, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1977-03
- Volume
- 74
- Issue
- 3
- Pages
- 801-805
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2055826882
- Cited by
- 217
- References
- 0
- FWCI
- 8.89
- Type
- journal article
- Language
- en
- Open access
- green
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: Mechanism of tertiary structural change in hemoglobin. https://app.cochat.ai/papers/10.1073/pnas.74.3.801
- The paper
- Gelin, B. R., & Karplus, M. (1977). Mechanism of tertiary structural change in hemoglobin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.74.3.801
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.
