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Cited by 300

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 access
Hill, R. Blake, Raleigh, Daniel P., Lombardi, Angela, DeGrado, William F.·2000·Accounts of Chemical Research

Abstract

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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Crossref · 10.1021/ar970004h

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Metadata

Authors
Hill, R. B., Raleigh, D. P., Lombardi, A., & DeGrado, W. F.
Venue
Accounts of Chemical Research
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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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.