The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Folding funnels and frustration in off-lattice minimalist protein landscapes
Open accessAbstract
A full quantitative understanding of the protein folding problem is now becoming possible with the help of the energy landscape theory and the protein folding funnel concept. Good folding sequences have a landscape that resembles a rough funnel where the energy bias towards the native state is larger than its ruggedness. Such a landscape leads not only to fast folding and stable native conformations but, more importantly, to sequences that are robust to variations in the protein environment and to sequence mutations. In this paper, an off-lattice model of sequences that fold into a β-barrel native structure is used to describe a framework that can quantitatively distinguish good and bad folders. The two sequences analyzed have the same native structure, but one of them is minimally frustrated whereas the other one exhibits a high degree of frustration.
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Cites
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
Self-citationFrom Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Self-citationToward an outline of the topography of a realistic protein-folding funnel.
Onuchic, J. N., Wolynes, P. G., Luthey-Schulten, Z., & Socci, N. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3626 · Cited by 523
Self-citationThe nature of folded states of globular proteins
Honeycutt, J. D., & Thirumalai, D. (1992) · Biopolymers · doi:10.1002/bip.360320610 · Cited by 360
Cited by
Clementi, C., Nymeyer, H., & Onuchic, J. N. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3693 · Cited by 1,240
Self-citationPerspective: Coarse-grained models for biomolecular systems
Noid, W. G. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4818908 · Cited by 893
Native contacts determine protein folding mechanisms in atomistic simulations
Best, R. B., Hummer, G., & Eaton, W. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311599110 · Cited by 594
Cheung, M. S., García, A. E., & Onuchic, J. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022387699 · Cited by 507
Self-citationThe origins of asymmetry in the folding transition states of protein L and protein G
Karanicolas, J., & Brooks, C. L. (2002) · Protein Science · doi:10.1110/ps.0205402 · Cited by 384
Metadata
- Authors
- Nymeyer, H., García, A. E., & Onuchic, J. N.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-05-26
- Volume
- 95
- Issue
- 11
- Pages
- 5921-5928
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1993321394
- Cited by
- 326
- References
- 5
- FWCI
- 8.10
- Type
- journal article
- Language
- en
- Open access
- green
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- Nymeyer, H., García, A. E., & Onuchic, J. N. (1998). Folding funnels and frustration in off-lattice minimalist protein landscapes. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.11.5921
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