Literature DB >> 3964288

The distances separating Tyr-69 from the high-affinity nucleotide and metal binding sites in actin.

J A Barden, M Miki.   

Abstract

The nucleotide binding site in actin was occupied with the fluorescent analogue formycin A 5' triphosphate which acted as a fluorescent donor for the acceptor chromophore dansyl chloride attached to Tyr-69. The distance separating the two chromophores was calculated to be 2.1 nm from the fluorescence energy transfer measurements. Similar measurements were made of the distances separating dansyl chloride, acting as donor, on Tyr-69 from Co2+ occupying the metal binding site. A distance of 2.1 nm was similarly obtained.

Entities:  

Mesh:

Substances:

Year:  1986        PMID: 3964288

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  2 in total

Review 1.  Structure of actin observed by fluorescence resonance energy transfer spectroscopy.

Authors:  M Miki; S I O'Donoghue; C G Dos Remedios
Journal:  J Muscle Res Cell Motil       Date:  1992-04       Impact factor: 2.698

Review 2.  Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation.

Authors:  C G dos Remedios; M Miki; J A Barden
Journal:  J Muscle Res Cell Motil       Date:  1987-04       Impact factor: 2.698

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.