The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
STUDIES ON PROTEIN FOLDING, UNFOLDING AND FLUCTUATIONS BY COMPUTER SIMULATION: I. The effect of specific amino acid sequence represented by specific inter‐unit interactions
Abstract
A lattice model of proteins is introduced. “A protein molecule” is a chain of non‐intersecting units of a given length on the two‐dimensional square lattice. The copolymeric character of protein molecules is incorporated into the model in the form of specificities of inter‐unit interactions. This model proved most effective for studying the statistical mechanical characteristics of protein folding, unfolding and fluctuations. The specificities of inter‐unit interactions are shown to be the primary factors responsible for the all‐or‐none type transition from native to denatured states of globular proteins. The model has been studied by the Monte Carlo method of Metropolis et al., which is now shown applied to approximately simulating a kinetic process. In the strong limit of the specificity of the inter‐unit interaction the native conformation was reached in this method by starting from an extended conformation. The possible generalization and application of this method for finding the native conformation of proteins from their amino acid sequence are discussed.
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Cites
Equation of State Calculations by Fast Computing Machines
Metropolis, N., Rosenbluth, A. W., Rosenbluth, M. N., Teller, A. H., & Teller, E. (1953) · The Journal of Chemical Physics · doi:10.1063/1.1699114 · Cited by 37,192
Cited by
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
Principles of protein folding — A perspective from simple exact models
Dill, K. A., Bromberg, S., Yue, K., Chan, H. S., Fiebig, K. M., Yee, D. P., & Thomas, P. D. (1995) · Protein Science · doi:10.1002/pro.5560040401 · Cited by 1,525
Perspective: 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
Normal Mode Analysis of Biomolecular Structures: Functional Mechanisms of Membrane Proteins
Bahar, I., Lezon, T. R., Bakan, A., & Shrivastava, I. H. (2010) · Chemical Reviews · doi:10.1021/cr900095e · Cited by 537
Metadata
- Authors
- Taketomi, H., Ueda, Y., & Gō, N.
- Venue
- International Journal of Peptide and Protein Research
- Publisher
- Wiley
- Published
- 1975-11
- Volume
- 7
- Issue
- 6
- Pages
- 445-459
- ISSN
- 0367-8377 (ISSN-L)
- OpenAlex
- W1550166367
- Cited by
- 674
- References
- 1
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: STUDIES ON PROTEIN FOLDING, UNFOLDING AND FLUCTUATIONS BY COMPUTER SIMULATION: I. The effect of specific amino acid sequence represented by specific inter‐unit interactions. https://app.cochat.ai/papers/10.1111/j.1399-3011.1975.tb02465.x
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- Taketomi, H., Ueda, Y., & Gō, N. (1975). STUDIES ON PROTEIN FOLDING, UNFOLDING AND FLUCTUATIONS BY COMPUTER SIMULATION: I. The effect of specific amino acid sequence represented by specific inter‐unit interactions. International Journal of Peptide and Protein Research. https://doi.org/10.1111/j.1399-3011.1975.tb02465.x
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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.
