The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Protein Design: A Hierarchic Approach
Abstract
The de novo design of peptides and proteins has recently emerged as an approach for investigating protein structure and function. Designed, helical peptides provide model systems for dissecting and quantifying the multiple interactions that stabilize secondary structure formation. De novo design is also useful for exploring the features that specify the stoichiometry and stability of α-helical coiled coils and for defining the requirements for folding into structures that resemble native, functional proteins. The design process often occurs in a series of discrete steps. Such steps reflect the hierarchy of forces required for stabilizing tertiary structures, beginning with hydrophobic forces and adding more specific interactions as required to achieve a unique, functional protein.
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Cites
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
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Toward an outline of the topography of a realistic protein-folding funnel.
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Crystal structure of an isoleucine-zipper trimer
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In vivo repression by a site-specific DNA-binding protein designed against an oncogenic sequence
Choo, Y., Sánchez-García, I., & Klug, A. (1994) · Nature · doi:10.1038/372642a0 · Cited by 292
LINUS: a hierarchic procedure to predict the fold of a protein
Srinivasan, R., & Rose, G. D. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340220202 · Cited by 266
Cited by
Controlling Allosteric Networks in Proteins
Dokholyan, N. V. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00544 · Cited by 260
Ambroggio, X. I., & Kuhlman, B. (2006) · Journal of the American Chemical Society · doi:10.1021/ja054718w · Cited by 200
Accola, M. A., Höglund, S., & Göttlinger, H. G. (1998) · Journal of Virology · doi:10.1128/jvi.72.3.2072-2078.1998 · Cited by 196
Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils
Woolfson, D. N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104579 · Cited by 106
“As reviewed elsewhere (70, 146, 147), these have been design targets for DeGrado, Dutton, their former group Left-hand column, systematic name of the de novo coiled-coil assembly (Fig.”
The emergence of life on Earth
Lahav, N., Nir, S., & Elitzur, A. C. (2001) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(01)00003-7 · Cited by 73
Metadata
- Authors
- Bryson, J. W., Betz, S. F., Lu, H. S., Suich, D. J., Zhou, H. X., O'Neil, K. T., & DeGrado, W. F.
- Venue
- Science
- Published
- 1995-11-10
- Volume
- 270
- Issue
- 5238
- Pages
- 935-941
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2088409695
- Cited by
- 530
- References
- 6
- FWCI
- 15.99
- Type
- journal article
- Language
- en
- Open access
- closed
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- Bryson, J. W., Betz, S. F., Lu, H. S., Suich, D. J., Zhou, H. X., O'Neil, K. T., & DeGrado, W. F. (1995). Protein Design: A Hierarchic Approach. Science. https://doi.org/10.1126/science.270.5238.935
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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.
