The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Understanding β-hairpin formation
Open accessAbstract
The kinetics of formation of protein structural motifs (e.g., α-helices and β-hairpins) can provide information about the early events in protein folding. A recent study has used fluorescence measurements to monitor the folding thermodynamics and kinetics of a 16-residue β-hairpin. In the present paper, we obtain the free energy surface and conformations involved in the folding of an atomistic model for the β-hairpin from multicanonical Monte Carlo simulations. The results suggest that folding proceeds by a collapse that is downhill in free energy, followed by rearrangement to form a structure with part of the hydrophobic cluster; the hairpin hydrogen bonds propagate outwards in both directions from the partial cluster. Such a folding mechanism differs from the published interpretation of the experimental results, which is based on a helix–coil-type phenomenological model.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) · Journal of Computational Chemistry · doi:10.1002/jcc.540040211 · Cited by 14,944
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
Hydrophobicity at Small and Large Length Scales
Lum, K., Chandler, D., & Weeks, J. D. (1999) · The Journal of Physical Chemistry B · doi:10.1021/jp984327m · Cited by 1,670
Multicanonical ensemble: A new approach to simulate first-order phase transitions
Berg, B. A., & Neuhaus, T. (1992) · Physical Review Letters · doi:10.1103/physrevlett.68.9 · Cited by 1,581
Simulation of activation free energies in molecular systems
Neria, E., Fischer, S., & Karplus, M. (1996) · The Journal of Chemical Physics · doi:10.1063/1.472061 · Cited by 1,322
Self-citationEffective energy function for proteins in solution
Lazaridis, T., & Karplus, M. (1999) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19990501)35:2<133::aid-prot1>3.0.co;2-n · Cited by 1,269
Self-citationWolynes, P. G., Onuchic, J. N., & Thirumalai, D. (1995) · Science · doi:10.1126/science.7886447 · Cited by 1,200
Folding dynamics and mechanism of β-hairpin formation
Muñoz, V., Thompson, P. A., Hofrichter, J., & Eaton, W. A. (1997) · Nature · doi:10.1038/36626 · Cited by 929
Protein Folding: A Perspective from Theory and Experiment
Dobson, C. M., Šali, A., & Karplus, M. (1998) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19980420)37:7<868::aid-anie868>3.0.co;2-h · Cited by 869
Self-citationA Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G
Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M., Wingfield, P. T., & Clore, G. M. (1991) · Science · doi:10.1126/science.1871600 · Cited by 816
Cited by
Gallicchio, E., & Levy, R. M. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.10400 · Cited by 328
Protein Design: From the Aspect of Water Solubility and Stability
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A., & Zhang, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 312
Force Generation in Kinesin Hinges on Cover-Neck Bundle Formation
Hwang, W., Lang, M. J., & Karplus, M. (2008) · Structure · doi:10.1016/j.str.2007.11.008 · Cited by 161
Self-citationThe Unfolded Ensemble and Folding Mechanism of the C-Terminal GB1 β-Hairpin
Bonomi, M., Branduardi, D., Gervasio, F. L., & Parrinello, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803652f · Cited by 97
Metadata
- Authors
- Dinner, A. R., Lazaridis, T., & Karplus, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-08-03
- Volume
- 96
- Issue
- 16
- Pages
- 9068-9073
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2066010782
- Cited by
- 326
- References
- 32
- FWCI
- 6.20
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Understanding β-hairpin formation. https://app.cochat.ai/papers/10.1073/pnas.96.16.9068
- The paper
- Dinner, A. R., Lazaridis, T., & Karplus, M. (1999). Understanding β-hairpin formation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.16.9068
Data sources
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.
