The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function
Open accessAbstract
De novo protein design has proven to be a powerful tool for understanding protein folding, structure, and function. In this Account, we highlight aspects of our research on the design of dimeric, four-helix bundles. Dimeric, four-helix bundles are found throughout nature, and the history of their design in our laboratory illustrates our hierarchic approach to protein design. This approach has been successfully applied to create a completely native-like protein. Structural and mutational analysis allowed us to explore the determinants of native protein structure. These determinants were then applied to the design of a dinuclear metal-binding protein that can now serve as a model for this important class of proteins.
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Cites
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The Design of Coiled-Coil Structures and Assemblies
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Principles for designing ideal protein structures
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Protein Design: Toward Functional Metalloenzymes
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Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils
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Navigating the Structural Landscape of De Novo α-Helical Bundles
Rhys, G. G., Wood, C. W., Beesley, J. L., Zaccai, N. R., Burton, A. J., Brady, R. L., Thomson, A. R., & Woolfson, D. N. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13354 · Cited by 48
Metadata
- Authors
- Hill, R. B., Raleigh, D. P., Lombardi, A., & DeGrado, W. F.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-10-24
- Volume
- 33
- Issue
- 11
- Pages
- 745-754
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2090265120
- Cited by
- 300
- References
- 104
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- green
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