July 25, 2008BiochemistryOpen Access

The N-Terminus of Apolipoprotein A-V Adopts a Helix Bundle Molecular Architecture

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Population

Recombinant human apolipoprotein A-V variants (apoA-V and apoA-V) expressed in Escherichia coli

Comparison

Structural and biochemical analysis vs Full-length apoA-V

Design

Preclinical

Authors

KWKasuen WongUniversity of Alberta JBJennifer A. BecksteadSana Biotechnology (United States)DLDustin LeeJohns Hopkins University

Discussion

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Implication

apoA-V N-terminal helix bundle informs structural models; leaves open relevance to human triglyceride disorders pending validation.

Structured PICO

Population

Recombinant human apolipoprotein A-V (apoA-V) variants (apoA-V(1-146) and apoA-V(1-169)) expressed in Escherichia coli

Intervention

Structural and biochemical analysis (sedimentation equilibrium, guanidine HCl denaturation, fluorescence quenching)

Comparator

Full-length apoA-V

Outcome

Molecular architecture and folding properties of the N-terminal fragmentsurrogate

The N-terminal domain of human apolipoprotein A-V independently folds into a helix bundle architecture, providing insight into its structural biology.

Cite This Study

Wong et al. (2008) studied this question.

synapsesocial.com/papers/6a886dc1d03e68c3c9a555d2 https://doi.org/10.1021/bi800515c

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The N-Terminus of Apolipoprotein A-V Adopts a Helix Bundle Molecular Architecture

Discussion

Member takes

Implication

Structured PICO

Cite This Study

The N-Terminus of Apolipoprotein A-V Adopts a Helix Bundle Molecular Architecture

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider