By the same authors

From the same journal

RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-α-HELIX BUNDLE

Research output: Contribution to journalArticle

Author(s)

  • M VLASSI
  • C STEIF
  • P WEBER
  • D TSERNOGLOU
  • K S WILSON
  • H J HINZ
  • M KOKKINIDIS

Department/unit(s)

Publication details

JournalNature Structural Biology
DatePublished - Oct 1994
Issue number10
Volume1
Number of pages11
Pages (from-to)706-716
Original languageEnglish

Abstract

The sequences of alpha-helical coiled-coils and bundles are characterized by a specific pattern of hydrophobic and hydrophilic residues which is repeated every seven residues. Highly conserved breaks in this pattern frecquently occur in segments of otherwise continuous heptad substructures. The hairpin bend of the ROP protein coincides with such a break and provides a model system for the study of the structural effects induced by heptad discontinuities. The structure of a ROP mutant which re-establishes a continuous heptad pattern, shows insignificant changes relative to the wild-type protein, as is also reflected in its conformational stability, spectroscopic properties and unfolding behaviour Thus, formation of alpha-alpha-hairpin bends may occur both in the presence and absence of heptad breaks.

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