Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin
Open accessAbstract
The transition state for the R in equilibrium with T quaternary conformational change of hemoglobin has thermodynamic properties much closer to those of the R conformation than to those of the T conformation. This finding is based on a comparison of activation and equilibrium enthalpy and entropy changes and on the observation of a linear free energy relationship between quaternary rate and equilibrium constants. A previous theoretical study [Janin, J. & Wodak, S. J. (1985) Biopolymers 24, 509-526], using a highly simplified energy function, suggests that the R-like transition state is the result of a reaction pathway with the maximum buried surface area between alpha beta dimers.
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- Authors
- Eaton, W. A., Henry, E. R., & Hofrichter, J.
- Affiliations
- National Institutes of Health (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1991-05-15
- Volume
- 88
- Issue
- 10
- Pages
- 4472-4475
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC51682
- OpenAlex
- W2000782090
- Cited by
- 72
- References
- 35
- Citations by year
- 2023: 4 · 2021: 3 · 2020: 5 · 2019: 3 · 2016: 1 · 2015: 2 · 2014: 1 · 2013: 3
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › thermodynamics and calorimetric analyses
- Keywords
- hemoglobin, quaternary structure, R state, T state, conformational change, transition state, linear free energy relationships, activation enthalpy, activation entropy, alpha beta dimer, buried surface area, protein conformational dynamics
- MeSH terms
- Allosteric Regulation, Hemoglobins, Humans, Kinetics, Protein Conformation, Thermodynamics, Macromolecular Substances
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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 ›
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