April 1, 1993Journal of Biological ChemistryOpen Access

Kinetics of structural changes of reconstituted skeletal muscle thin filaments observed by fluorescence resonance energy transfer.

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Population

Reconstituted skeletal muscle thin filaments

Comparison

Changes in free Ca2+ concentration vs Presence vs absence of Ca2+

Design

Preclinical

Authors

MMMasao MikiUniversity of Fukui TITakayoshi IioNagoya University

Discussion

Member takes

Implication

Does not alter clinical practice; extends FRET evidence for troponin-tropomyosin regulation in skeletal thin filaments.

Structured PICO

Population

Reconstituted skeletal muscle thin filaments (Troponin-I labeled with 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid, and actin labeled with fluorescein 5-isothiocyanate)

Intervention

Changes in free Ca2+ concentration (rapid increase or decrease)

Comparator

Presence vs absence of Ca2+

Outcome

Efficiency of resonance energy transfer and rate constants of fluorescence intensity changesurrogate

The conformational changes observed by FRET in reconstituted skeletal muscle thin filaments correspond well to the regulation mechanism by troponin-tropomyosin.

Cite This Study

Miki et al. (1993) studied this question.

synapsesocial.com/papers/6a71432026a7f98052dda4b3 https://doi.org/10.1016/s0021-9258(18)53151-3

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Kinetics of structural changes of reconstituted skeletal muscle thin filaments observed by fluorescence resonance energy transfer.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Kinetics of structural changes of reconstituted skeletal muscle thin filaments observed by fluorescence resonance energy transfer.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider