The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Vibrational Dynamics of Folded Proteins: Significance of Slow and Fast Motions in Relation to Function and Stability
Abstract
A single-parameter harmonic Hamiltonian based on local packing density and contact topology is proposed for studying residue fluctuations in native proteins. The internal energy obeys an equipartition law, and free energy changes result from entropy fluctuations only. Frequency--wave-number maps show communication between residues involved in slow and fast modes. Fast modes are strongly localized, resulting from the geometric irregularity of the structure. Comparison with experiments shows that slow and fast modes are associated, respectively, with function and stability. Specifically, domain motions and folding cores of HIV-1 protease are accurately identified.
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Citations
Cites
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Anderson, P. W. (1958) · Physical Review · doi:10.1103/physrev.109.1492 · Cited by 12,468
Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis
Tirion, M. M. (1996) · Physical Review Letters · doi:10.1103/physrevlett.77.1905 · Cited by 1,615
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Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
Bahar, I., Atilgan, A. R., & Erman, B. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00024-2 · Cited by 1,375
Self-citationMethod for estimating the configurational entropy of macromolecules
Karplus, M., & Kushick, J. N. (1981) · Macromolecules · doi:10.1021/ma50003a019 · Cited by 849
Gaussian Dynamics of Folded Proteins
Haliloglu, T., Bahar, I., & Erman, B. (1997) · Physical Review Letters · doi:10.1103/physrevlett.79.3090 · Cited by 772
Self-citationStatistical thermodynamics of random networks
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Systematic mutation of bacteriophage T4 lysozyme
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Complete mutagenesis of the HIV-1 protease
Loeb, D. D., Swanstrom, R., Everitt, L., Manchester, M., Stamper, S. E., & Hutchison, C. A. (1989) · Nature · doi:10.1038/340397a0 · Cited by 327
Local moments and localized states
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Cited by
Global dynamics of proteins: bridging between structure and function
Bahar, I., Lezon, T. R., Yang, L.-W., & Eyal, E. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.093008.131258 · Cited by 610
Self-citationGlobal ribosome motions revealed with elastic network model
Wang, Y., Rader, A. J., Bahar, I., & Jernigan, R. L. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.01.005 · Cited by 284
Self-citationYang, L.-W., & Bahar, I. (2005) · Structure · doi:10.1016/j.str.2005.03.015 · Cited by 273
Self-citationPersistent homology analysis of protein structure, flexibility, and folding
Xia, K., & Wei, G. (2014) · International Journal for Numerical Methods in Biomedical Engineering · doi:10.1002/cnm.2655 · Cited by 254
The Role of Conformational Dynamics and Allostery in Modulating Protein Evolution
Campitelli, P., Modi, T., Kumar, S., & Ozkan, S. B. (2020) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115517 · Cited by 190
Metadata
- Authors
- Bahar, I., Atilgan, A. R., Demirel, M. C., & Erman, B.
- Venue
- Physical Review Letters
- Publisher
- American Physical Society (APS)
- Published
- 1998-03-23
- Volume
- 80
- Issue
- 12
- Pages
- 2733-2736
- ISSN
- 0031-9007 (ISSN-L)
- 1079-7114
- OpenAlex
- W2044877050
- Cited by
- 441
- References
- 19
- FWCI
- 2.59
- Type
- journal article
- Language
- en
- Open access
- closed
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- The paper
- Bahar, I., Atilgan, A. R., Demirel, M. C., & Erman, B. (1998). Vibrational Dynamics of Folded Proteins: Significance of Slow and Fast Motions in Relation to Function and Stability. Physical Review Letters. https://doi.org/10.1103/physrevlett.80.2733
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
