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May 1, 1987Journal of Biological ChemistryOpen Access

The conformation of cross-linked actin·S-1 in the presence and absence of ATP.

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Population

Biochemical model (myosin subfragment 1 (S-1) cross-linked to actin, troponin-tropomyosin-actin complex)

Design

Preclinical

Authors

RKRobert Thomas KingNational Institutes of HealthLGLois E. GreeneNational Institutes of Health

Discussion

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Implication

Supports alternating cross-bridge conformations in vitro; leaves open relevance to intact cardiac muscle in vivo.

Structured PICO

P
Population
Biochemical model (myosin subfragment 1 (S-1) cross-linked to actin, troponin-tropomyosin-actin complex)
I
Intervention
Modification of S-1 with NEM or pPDM and cross-linking to actin in the presence or absence of ATP/ADP
O
Outcome
Conformation of the cross-linked actin·S-1 complexes (weak-binding vs strong-binding conformation)surrogate

Biochemical evidence supports that the cross-linked actin·S-1 complex can alternate between weak-binding and strong-binding conformations during the cross-bridge cycle.

Cite This Study

King et al. (1987) studied this question.

synapsesocial.com/papers/6a71432178a11c550e0b5000https://doi.org/10.1016/s0021-9258(18)45547-0
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Mechanism of inhibition of relaxation by N-ethylmaleimide treatment of myosin1976 · 76 citations
  2. 2Effect of nucleotide on the binding of N-N'-p-Phenylenedimaleimide-modified S-1 to unregulated and regulated actin1986 · 26 citations
  3. 3Regulation of the ATPase activity of cross-linked actin-myosin subfragment 1 by troponin-tropomyosin1985 · 18 citations
  4. 4Structure of the actin-myosin complex in the presence of ATP.1985 · 81 citations
  5. 5Binding of ADP and ATP analogs to cross-linked and non-cross-linked acto X S-1.1986 · 27 citations