The DOI matches its Crossref record.
Internal Stark Effect Measurement of the Electric Field at the Amino Terminus of an α Helix
Abstract
The strengths of electrostatic interactions in biological molecules are difficult to calculate or predict because they occur in complicated, inhomogeneous environments. The electric field at the amino terminus of an α helix in water has been determined by measuring the shift in the absorption band for a covalently attached, neutral probe molecule with an electric dipole moment difference between the ground and excited electronic states (an internal Stark effect). The field at the interface between the helix and the solvent is found to be an order of magnitude stronger than expected from the dielectric properties of bulk water. Furthermore, although the total electric dipole moment of the helix increases with length, the electric field at the amino terminus does not.
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
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
Self-citationMechanisms of Tryptophan Fluorescence Shifts in Proteins
Vivian, J. T., & Callis, P. R. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76183-8 · Cited by 1,493
Exploring the Helix-Coil Transition via All-Atom Equilibrium Ensemble Simulations
Sorin, E. J., & Pande, V. S. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.051938 · Cited by 648
Chodera, J. D., Singhal, N., Pande, V. S., Dill, K. A., & Swope, W. C. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2714538 · Cited by 640
High-Resolution Protein Design with Backbone Freedom
Harbury, P. B., Plecs, J. J., Tidor, B., Alber, T., & Kim, P. S. (1998) · Science · doi:10.1126/science.282.5393.1462 · Cited by 458
Self-citation
Metadata
- Authors
- Lockhart, D. J., & Kim, P. S.
- Venue
- Science
- Published
- 1992-08-14
- Volume
- 257
- Issue
- 5072
- Pages
- 947-951
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2030852504
- Cited by
- 263
- References
- 0
- FWCI
- 3.05
- 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: Internal Stark Effect Measurement of the Electric Field at the Amino Terminus of an α Helix. https://app.cochat.ai/papers/10.1126/science.1502559
- The paper
- Lockhart, D. J., & Kim, P. S. (1992). Internal Stark Effect Measurement of the Electric Field at the Amino Terminus of an α Helix. Science. https://doi.org/10.1126/science.1502559
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.
