Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 420

The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.

Protein Folding in the Hydrophobic-Hydrophilic ( HP ) Model is NP-Complete

BERGER, BONNIE, LEIGHTON, TOM·1998·Journal of Computational Biology

Abstract

One of the simplest and most popular biophysical models of protein folding is the hydrophobic-hydrophilic (HP) model. The HP model abstracts the hydrophobic interaction in protein folding by labeling the amino acids as hydrophobic (H for nonpolar) or hydrophilic (P for polar). Chains of amino acids are configured as self-avoiding walks on the 3D cubic lattice, where an optimal conformation maximizes the number of adjacencies between H's. In this paper, the protein folding problem under the HP model on the cubic lattice is shown to be NP-complete. This means that the protein folding problem belongs to a large set of problems that are believed to be computationally intractable.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1089/cmb.1998.5.27

Cites

11 of 11 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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

Show all 11 references

Cited by

See all 420

Metadata

Authors
BERGER, B., & LEIGHTON, T.
Venue
Journal of Computational Biology
Published
1998-01
Volume
5
Issue
1
Pages
27-40
ISSN
  • 1066-5277 (ISSN-L)
  • 1557-8666
OpenAlex
W2611927968
Cited by
420
References
11
FWCI
2.03
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: Protein Folding in the Hydrophobic-Hydrophilic ( HP ) Model is NP-Complete. https://app.cochat.ai/papers/10.1089/cmb.1998.5.27
The paper
BERGER, B., & LEIGHTON, T. (1998). Protein Folding in the Hydrophobic-Hydrophilic ( HP ) Model is NP-Complete. Journal of Computational Biology. https://doi.org/10.1089/cmb.1998.5.27

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.