The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Relating Protein Motion to Catalysis
Abstract
This review examines the linkage between protein conformational motions and enzyme catalysis. The fundamental issues related to this linkage are probed in the context of two enzymes that catalyze hydride transfer, namely dihydrofolate reductase and liver alcohol dehydrogenase. The extensive experimental and theoretical studies addressing the role of protein conformational changes in these enzyme reactions are summarized. Evidence is presented for a network of coupled motions throughout the protein fold that facilitate the chemical reaction. This network is comprised of fast thermal motions that are in equilibrium as the reaction progresses along the reaction coordinate and that lead to slower equilibrium conformational changes conducive to the chemical reaction.
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
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Cited by
The Methylation Effect in Medicinal Chemistry
Barreiro, E. J., Kümmerle, A. E., & Fraga, C. A. M. (2011) · Chemical Reviews · doi:10.1021/cr200060g · Cited by 1,017
The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis
Boehr, D. D., McElheny, D., Dyson, H. J., & Wright, P. E. (2006) · Science · doi:10.1126/science.1130258 · Cited by 957
Norris, V., Krylov, S. N., Agarwal, P. K., & White, G. J. (2017) · Microbial Physiology · doi:10.1159/000464443 · Cited by 632
Reetz, M. T. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201000826 · Cited by 538
Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
Bahar, I., Chennubhotla, C., & Tobi, D. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.09.011 · Cited by 306
Metadata
- Authors
- Hammes-Schiffer, S., & Benkovic, S. J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2006-06-01
- Volume
- 75
- Issue
- 1
- Pages
- 519-541
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2008609697
- Cited by
- 610
- References
- 1
- FWCI
- 2.43
- 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: Relating Protein Motion to Catalysis. https://app.cochat.ai/papers/10.1146/annurev.biochem.75.103004.142800
- The paper
- Hammes-Schiffer, S., & Benkovic, S. J. (2006). Relating Protein Motion to Catalysis. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.75.103004.142800
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.
