The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
Open accessAbstract
Here we describe how the systematic redesign of a protein's hydrophobic core alters its structure and stability. We have repacked the hydrophobic core of the four‐helix‐bundle protein, Rop, with altered packing patterns and various side chain shapes and sizes. Several designs reproduce the structure and native‐like properties of the wild‐type, while increasing the thermal stability. Other designs, either with similar sizes but different shapes, or with decreased sizes of the packing residues, destabilize the protein. Finally, overpacking the core with larger side chains causes a loss of native‐like structure. These results allow us to further define the roles of tight residue packing and the burial of hydrophobic surface area in the construction of native‐like proteins.
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Citations
Cites
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490 · cited 1×
“By contrast, the packing of residues in the hydrophobic core appears to be extremely important for the structure, stability, and native-like properties of natural proteins (Kellis et al., 1989; Shortle et al., 1990; Sandberg & Terwilliger, 1991; Eriksson et al., 1992; Baldwin et al., 1993; Harbury et al., 1993; Jackso…”
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Cited by
Wei, K. Y., Moschidi, D., Bick, M. J., Nerli, S., McShan, A. C., Carter, L. P., Huang, P.-S., Fletcher, D. A., Sgourakis, N. G., Boyken, S. E., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914808117 · Cited by 57
Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex
Kao, C.-F., Liu, C.-Y., Hsieh, C.-L., Carillo, K. J. D., Tzou, D.-L. M., Wang, H.-C., & Chang, W. (2023) · Journal of Virology · doi:10.1128/jvi.01343-23 · Cited by 12
Curti, M., Maffeis, V., Teixeira Alves Duarte, L. G., Shareef, S., Hallado, L. X., Curutchet, C., & Romero, E. (2023) · Protein Science · doi:10.1002/pro.4579 · Cited by 10
Metadata
- Authors
- Munson, M., Balasubramanian, S., Fleming, K. G., Nagi, A. D., O'Brien, R., Sturtevant, J. M., & Regan, L.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 1996-08
- Volume
- 5
- Issue
- 8
- Pages
- 1584-1593
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2165740393
- Cited by
- 194
- References
- 1
- FWCI
- 5.07
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Munson, M., Balasubramanian, S., Fleming, K. G., Nagi, A. D., O'Brien, R., Sturtevant, J. M., & Regan, L. (1996). What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Science. https://doi.org/10.1002/pro.5560050813
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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.
