A study of four-helix bundles: Investigating protein folding via similar architectural motifs in protein cores and in subunit interfaces

Shuo Liang Lin*, Chung Jung Tsai, Ruth Nussinov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Four-helix bundles are identified and characterized in the subunit interfaces of protein multimers. We find that this motif occurs as often in the interfaces as in the protein monomers. Common and different characteristics demonstrated by the bundles in the two environments suggest the possible stabilization mechanisms of the bundles via cooperative helical twist, dipole alignment and interhelical connections. Nucleation of parallel helix pairs may be a favourable pathway before the pairs couple into bundles during folding. Certain properties found chaotic in the interface four-helix bundles indicate that either the subunit association is far from the global minimum conformation, or that the footprints of the folding pathway are recorded in these properties.

Original languageEnglish
Pages (from-to)151-161
Number of pages11
JournalJournal of Molecular Biology
Volume248
Issue number1
DOIs
StatePublished - 21 Apr 1995

Funding

FundersFunder number
U.S. Department of Health and Human Services1-CO-74102, 91-00219
National Cancer Institute
Academy of Leisure Sciences
United States-Israel Binational Science Foundation
Israel Science Foundation

    Keywords

    • Architectural motif
    • Four-helix bundle
    • Protein core
    • Protein folding
    • Subunit interface

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