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Native protein sequences are close to optimal for their structures
Open accessAbstract
How large is the volume of sequence space that is compatible with a given protein structure? Starting from random sequences, low free energy sequences were generated for 108 protein backbone structures by using a Monte Carlo optimization procedure and a free energy function based primarily on Lennard–Jones packing interactions and the Lazaridis–Karplus implicit solvation model. Remarkably, in the designed sequences 51% of the core residues and 27% of all residues were identical to the amino acids in the corresponding positions in the native sequences. The lowest free energy sequences obtained for ensembles of native-like backbone structures were also similar to the native sequence. Furthermore, both the individual residue frequencies and the covariances between pairs of positions observed in the very large SH3 domain family were recapitulated in core sequences designed for SH3 domain structures. Taken together, these results suggest that the volume of sequence space optimal for a protein structure is surprisingly restricted to a region around the native sequence.
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Citations
Cited by
Leaver-Fay (2011) · doi:10.1016/b978-0-12-381270-4.00019-6 · Cited by 1,904
The Rosetta All-Atom Energy Function for Macromolecular Modeling and Design
Alford, R. F., Leaver-Fay, A., Jeliazkov, J. R., O’Meara, M. J., DiMaio, F. P., Park, H., Shapovalov, M. V., Renfrew, P. D., Mulligan, V. K., Kappel, K., et al. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00125 · Cited by 1,532
Self-citationThe coming of age of de novo protein design
Huang, P.-S., Boyken, S. E., & Baker, D. (2016) · Nature · doi:10.1038/nature19946 · Cited by 1,478
Self-citationShapovalov, M. V., & Dunbrack, R. L. (2011) · Structure · doi:10.1016/j.str.2011.03.019 · Cited by 1,000
Consistent blind protein structure generation from NMR chemical shift data
Shen, Y., Lange, O., Delaglio, F., Rossi, P., Aramini, J. M., Liu, G., Eletsky, A., Wu, Y., Singarapu, K. K., Lemak, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800256105 · Cited by 855
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Metadata
- Authors
- Kuhlman, B., & Baker, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-09-12
- Volume
- 97
- Issue
- 19
- Pages
- 10383-10388
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2135815512
- Cited by
- 810
- References
- 0
- FWCI
- 5.75
- Type
- journal article
- Language
- en
- Open access
- green
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