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August 25, 2000Biochemistry

Modulation of Troponin T Molecular Conformation and Flexibility by Metal Ion Binding to the NH2-Terminal Variable Region

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Population

Chicken fast skeletal muscle TnT isoform, TnT8e16

Design

Preclinical

Authors

JJJian‐Ping JinHeart Failure & TransplantDRDouglas D. RootUniversity of North Texas

Discussion

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Implication

Should not change clinical troponin interpretation; extends prior binding studies but leaves open contractile effects in vivo.

Structured PICO

P
Population
Chicken fast skeletal muscle TnT isoform, TnT8e16
I
Intervention
Cu(II) binding titration
O
Outcome
Changes in fluorescence intensity and anisotropy of COOH-domain Trp residues and fluorescein-labeled Cys263surrogate

The alternatively spliced NH2-terminal variable region of Troponin T modulates the conformation and flexibility of other domains of the protein upon metal ion binding.

Cite This Study

Jin et al. (2000) studied this question.

synapsesocial.com/papers/6a19639fc3e09444f388cd75https://doi.org/10.1021/bi9927437
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Also Consider

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

  1. 1Developmentally Regulated, Alternative RNA Splicing-generated Pectoral Muscle-specific Troponin T Isoforms and Role of the NH2-terminal Hypervariable Region in the Tolerance to Acidosis1998 · 47 citations
  2. 2Structure-function studies of the amino-terminal region of bovine cardiac troponin T.1988 · 70 citations
  3. 3Acidic and basic troponin T isoforms in mature fast-twitch skeletal muscle and effect on contractility1999 · 84 citations
  4. 4The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C.1987 · 134 citations
  5. 5Functional Consequences of Troponin T Mutations Found in Hypertrophic Cardiomyopathy1999 · 87 citations