Satisfying turns in folding transitions

M. Gruebele, P. G. Wolynes

Research output: Contribution to journalArticlepeer-review

Abstract

Protein engineering studies show that conformations in the folding transition state ensemble can be structurally polarized. In two SH3 β-sheet domains, the formation of hydrophobic contacts goes hand in hand with the formation of the solvated distal loop β-turn, while large parts of the molecule remain unstructured in the ensemble.

Original languageEnglish (US)
Pages (from-to)662-665
Number of pages4
JournalNature Structural and Molecular Biology
Volume5
Issue number8
DOIs
StatePublished - Aug 1998

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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