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Cited by 1,303

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families

Lockless, Steve W., Ranganathan, Rama·1999·Science

Abstract

For mapping energetic interactions in proteins, a technique was developed that uses evolutionary data for a protein family to measure statistical interactions between amino acid positions. For the PDZ domain family, this analysis predicted a set of energetically coupled positions for a binding site residue that includes unexpected long-range interactions. Mutational studies confirm these predictions, demonstrating that the statistical energy function is a good indicator of thermodynamic coupling in proteins. Sets of interacting residues form connected pathways through the protein fold that may be the basis for efficient energy conduction within proteins.

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Metadata

Authors
Lockless, S. W., & Ranganathan, R.
Venue
Science
Published
1999-10-08
Volume
286
Issue
5438
Pages
295-299
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2092006899
Cited by
1,303
References
2
FWCI
4.35
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families. https://app.cochat.ai/papers/10.1126/science.286.5438.295
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Lockless, S. W., & Ranganathan, R. (1999). Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families. Science. https://doi.org/10.1126/science.286.5438.295

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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.