The core of apomyoglobin E-form folds at the diffusion limit

Rudolf Gilmanshin, Robert H. Callender, R. Brian Dyer

Research output: Contribution to journalLetter

40 Scopus citations

Abstract

The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15–20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 μs at 46 °C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation.

Original languageEnglish (US)
Pages (from-to)363-365
Number of pages3
JournalNature Structural Biology
Volume5
Issue number5
DOIs
StatePublished - May 1998

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

Fingerprint Dive into the research topics of 'The core of apomyoglobin E-form folds at the diffusion limit'. Together they form a unique fingerprint.

  • Cite this