October 27, 1998Proceedings of the National Academy of SciencesOpen Access

Smooth muscle myosin mutants containing a single tryptophan reveal molecular interactions at the actin-binding interface

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Population

Chicken gizzard smooth muscle myosin mutants

Comparison

Engineered mutants containing a single… vs Wild-type MDE

Design

Preclinical

Authors

CYChristopher M. YengoPennsylvania State University PFPatricia M. FagnantUniversity of Vermont LCLynn R. ChrinUniversity of Vermont

Discussion

Member takes

Implication

Does not yet guide clinical decisions; extends molecular mapping of the rigor acto-myosin interface for future modeling.

Structured PICO

Population

Chicken gizzard smooth muscle myosin mutants (truncated fragment including motor domain and essential light chain)

Intervention

Engineered mutants containing a single tryptophan at (Trp-546) or near (Trp-625) the putative actin-binding interface

Comparator

Wild-type MDE

Outcome

Fluorescence emission spectra and acrylamide quenching to assess structural changes at the actin-binding interfacesurrogate

This basic science study provides direct evidence for a specific molecular interaction between residues in the A-site of myosin and actin using engineered single-tryptophan mutants.

Cite This Study

Yengo et al. (1998) studied this question.

synapsesocial.com/papers/6a7043c1439bab0cabc31756 https://doi.org/10.1073/pnas.95.22.12944

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Smooth muscle myosin mutants containing a single tryptophan reveal molecular interactions at the actin-binding interface

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Smooth muscle myosin mutants containing a single tryptophan reveal molecular interactions at the actin-binding interface

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider