The DOI matches its Crossref record.
Molecular dynamics simulations of the unfolding of an .alpha.-helical analog of ribonuclease A S-peptide in water
Abstract
Molecular dynamics simulations of the S-peptide analogue AETAAAKFLREHMDS have been conducted in aqueous solution for 300 ps at 278 K and for 500 ps in two different runs at 358 K. The results show agreement with experimental observations in that at low temperature, 5 degrees C, the helix is stable, while unfolding is observed at 85 degrees C. In the low-temperature simulation a solvent-separated ion pair was formed between Glu-2 and Arg-10, and the side chain of His-12 reoriented toward the C-terminal end of the alpha-helix. Detailed analyses of the unfolding pathways at high temperature have also revealed that the formation or disappearance of main-chain helical hydrogen bonds occurs frequently through an alpha in equilibrium with 3(10) in equilibrium with no hydrogen bond sequence.
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
Cited by
Theoretical Methods for the Description of the Solvent Effect in Biomolecular Systems
Orozco, M., & Luque, F. J. (2000) · Chemical Reviews · doi:10.1021/cr990052a · Cited by 622
Shea, J.-E., & Brooks III, C. L. (2001) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.52.1.499 · Cited by 481
Definition and transfer of a serological epitope specific for peptide-empty forms of MHC class I
Yu, Y. Y. L., Myers, N. B., Hilbert, C. M., Harris, M. R., Balendiran, G. K., & Hansen, T. H. (1999) · International Immunology · doi:10.1093/intimm/11.12.1897 · Cited by 56
Metadata
- Authors
- Tirado-Rives, J., & Jorgensen, W. L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1991-04-23
- Volume
- 30
- Issue
- 16
- Pages
- 3864-3871
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2077042715
- Cited by
- 214
- References
- 0
- FWCI
- 6.22
- Type
- journal article
- Language
- en
- Open access
- closed
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: Molecular dynamics simulations of the unfolding of an .alpha.-helical analog of ribonuclease A S-peptide in water. https://app.cochat.ai/papers/10.1021/bi00230a009
- The paper
- Tirado-Rives, J., & Jorgensen, W. L. (1991). Molecular dynamics simulations of the unfolding of an .alpha.-helical analog of ribonuclease A S-peptide in water. Biochemistry. https://doi.org/10.1021/bi00230a009
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.
