On the possible origin of protein homochirality, structure, and biochemical function
Open accessAbstract
Significance: Living systems contain mainly chiral macromolecules, including proteins. How L-chiral proteins emerged from demi-chiral mixtures is unknown. Our simulations show that, compared to contemporary proteins, demi-chiral proteins have shorter regular secondary structures due to fewer internal hydrogen bonds, but similar global folds and small molecule binding sites. Demi-chiral proteins contain L-chiral substructures matching native active site geometries. Among the most frequently generated enzymes with native active site residues are ancient functions associated with metabolism and replication. This suggests that demi-chiral proteins could engage in early metabolism, creating the feedback loop for transcription and cell formation partly responsible for life’s emergence.
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Simulations recently suggested that 'demi-chiral' proteins exhibit structural requirements suitable for promoting early metabolism.
“simulations recently suggested that ''demi-chiral'' proteins, which contain a 1 : 1 ratio of (R) and (S) a-amino acids, even though less stable than their homochiral analogues, exhibit structural requirements (folding, substrate binding and active sites) suitable for promoting early metabolism”
From Possible chemical and physical scenarios towards biological homochirality (2022) · cites this paper as [557]
Cites
The antiquity of RNA-based evolution.
Joyce, G. F. (2002) · Nature · doi:10.1038/418214a · Cited by 1,070 · see citing works
Zhou, H., & Zhou, Y. (2002) · Protein Science · doi:10.1110/ps.0217002 · Cited by 902 · cited 1× · see citing works
“Finally, the DFIRE all-atom statistical potential (41) was employed to select the top polyleucine model for each protein.”
MethodSelf-citationProtocells and RNA Self-Replication
Joyce, G. F., & Szostak, J. W. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034801 · Cited by 308 · see citing works
Peptide ligation by chemoselective aminonitrile coupling in water
Canavelli, P., Islam, S., & Powner, M. W. (2019) · Nature · doi:10.1038/s41586-019-1371-4 · Cited by 188 · see citing works
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Possible chemical and physical scenarios towards biological homochirality
Sallembien, Q., Bouteiller, L., Crassous, J., & Raynal, M. (2022) · Chemical Society Reviews · doi:10.1039/d1cs01179k · Cited by 186 · see citing works
The role of local versus nonlocal physicochemical restraints in determining protein native structure
Skolnick, J., & Gao, M. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.008 · Cited by 21 · see citing works
Self-citation
- Authors
- Skolnick, J., Zhou, H., & Gao, M.
- Affiliations
- Georgia Institute of Technology (US)
- Corresponding author
- Skolnick, Jeffrey
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-12-10
- Volume
- 116
- Issue
- 52
- Pages
- 26571-26579
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6936705
- OpenAlex
- W2996547012
- Cited by
- 45
- References
- 4
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 9 · 2023: 7 · 2022: 9 · 2021: 7 · 2020: 4
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | National Institutes of Health (R35-118039)
- Topics
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- origin of life, L-amino acids, hydrogen bonding, protein stability, protein folding, enzyme active site, binding pocket, ribosomal proteins
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