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

R. Gilmanshin, Robert Callender, R. B. Dyer

Research output: Contribution to journalArticle

40 Citations (Scopus)

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 micros at 46 degrees 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
StatePublished - May 1998

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Fluorescence Spectrometry
Fluorescence spectroscopy
Infrared spectroscopy
Infrared radiation
Temperature
apomyoglobin

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

The core of apomyoglobin E-form folds at the diffusion limit. / Gilmanshin, R.; Callender, Robert; Dyer, R. B.

In: Nature Structural Biology, Vol. 5, No. 5, 05.1998, p. 363-365.

Research output: Contribution to journalArticle

Gilmanshin, R. ; Callender, Robert ; Dyer, R. B. / The core of apomyoglobin E-form folds at the diffusion limit. In: Nature Structural Biology. 1998 ; Vol. 5, No. 5. pp. 363-365.
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