The structure of cytochromec and the rates of molecular evolution
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The differences in characteristic rates of proteins could be explained by the proportion of neutral sites that each protein contained.
“Dickerson 5 compared what was then known about the protein structures of histones, cytochrome c , haemoglobins and fibrinopeptides, and concluded that their different rates of change could be explained by the proportion of neutral sites that each protein contained - the greater the proportion of neutral sites, the faster the rate of molecular evolution.”
From The modern molecular clock (2003) · cites this paper as [5]
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- Authors
- Dickerson, R. E.
- Affiliations
- California Institute of Technology (US)
- Corresponding author
- Dickerson, Richard E.
- Venue
- Journal of Molecular Evolution
- Published
- 1971-03
- Volume
- 1
- Issue
- 1
- Pages
- 26-45
- ISSN
- 0022-2844 (ISSN-L)
- 1432-1432
- OpenAlex
- W2008265915
- Cited by
- 544
- References
- 22
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 3 · 2023: 2 · 2022: 5 · 2021: 8 · 2020: 6 · 2019: 8 · 2018: 4 · 2017: 8 · 2016: 8 · 2015: 7 · 2014: 9 · 2013: 7 · 2012: 1
- FWCI
- 11.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Molecular Evolution (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Keywords
- cytochrome c, protein evolution rate, molecular evolution, protein structure, hydrophobic side chains, aromatic side chains, hydrophobic channels, cytochrome c reductase, cytochrome c oxidase, fibrinopeptides, globin, amino acid tolerance, protein function
- MeSH terms
- Amino Acid Sequence, Animals, Cytochrome c Group, Biological Evolution, Genes, Genetic Code, Hemoglobins, Humans, Mutation, Protein Conformation
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