August 9, 2006Archives of Biochemistry and BiophysicsOpen Access

Fluorescence labeling and computational analysis of the strut of myosin’s 50 kDa cleft

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Population

Myosin subfragment-1

Design

Preclinical

Authors

RGRavi K. GawalapuJackson State University DRDouglas D. RootUniversity of North Texas

Discussion

Member takes

Implication

May guide cardiac myosin research; leaves open relevance to human contractility or disease models.

Structured PICO

Population

Myosin subfragment-1

Intervention

Fluorescent labeling procedure using CY3 N-hydroxy succinimidyl ester and computational analysis (molecular mechanics and stochastic dynamics simulations)

Outcome

Labeling specificity, ATPase activity retention, fluorescence polarization changes upon actin/nucleotide binding, and simulated cleft movementsurrogate

A new fluorescent labeling procedure and computational analysis provide insights into the structural dynamics of myosin's 50 kDa cleft during actin binding.

Cite This Study

Gawalapu et al. (2006) studied this question.

synapsesocial.com/papers/6a71437efe4101aa97e07fc7 https://doi.org/10.1016/j.abb.2006.07.013

View Full Paper

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Fluorescence labeling and computational analysis of the strut of myosin’s 50 kDa cleft

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Fluorescence labeling and computational analysis of the strut of myosin’s 50 kDa cleft

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider