Protein tertiary structure recognition using optimized associative memory Hamiltonians

Richard A. Goldstein, Zaida A. Luthey-Schulten, Peter G. Wolynes

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Protein folding codes can be optimized using spin-glass theory. Simple optimal codes are deduced for associative memory Hamiltonians based on aligned sequences. The authors demonstrate the use of associate memory Hamiltonians and show how, with the use of spin-glass theory to provide optimization, and standard alignment methods, it is possible to generate an algorithm that correctly identifies structurally similar proteins in the vast majority of cases.

Original languageEnglish (US)
Title of host publicationProceedings of the 26th Hawaii International Conference on System Sciences, HICSS 1993
PublisherIEEE Computer Society
Pages699-707
Number of pages9
ISBN (Electronic)0818632305
DOIs
StatePublished - Jan 1 1993
Event26th Hawaii International Conference on System Sciences, HICSS 1993 - Wailea, United States
Duration: Jan 8 1993 → …

Publication series

NameProceedings of the Annual Hawaii International Conference on System Sciences
Volume1
ISSN (Print)1530-1605

Conference

Conference26th Hawaii International Conference on System Sciences, HICSS 1993
CountryUnited States
CityWailea
Period1/8/93 → …

ASJC Scopus subject areas

  • Engineering(all)

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  • Cite this

    Goldstein, R. A., Luthey-Schulten, Z. A., & Wolynes, P. G. (1993). Protein tertiary structure recognition using optimized associative memory Hamiltonians. In Proceedings of the 26th Hawaii International Conference on System Sciences, HICSS 1993 (pp. 699-707). [270671] (Proceedings of the Annual Hawaii International Conference on System Sciences; Vol. 1). IEEE Computer Society. https://doi.org/10.1109/HICSS.1993.270671