Evidence map›Paper›PMID 23518667›Full record

ArticleNature protocols2013

DNA nanotubes for NMR structure determination of membrane proteins.

Gaëtan Bellot, Mark A McClintock, James J Chou, William M Shih

Abstract read
In one paragraph

Article in Nature protocols, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. DNA Origami: Recent Progress and Applications.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Recent Progress of Magnetically Actuated DNA Micro/Nanorobots.Cyborg and bionic systems (Washington, D.C.) · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Facile and scalable preparation of pure and dense DNA origami solutions.Angewandte Chemie (International ed. in English) · 2014
    Article
  17. Amphipols for each season.The Journal of membrane biology · 2014
    Review
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Gaëtan Bellot1] Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA. [2] Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA. [3] Wyss Institute for Biologically Inspired Engineering at Harvard, Boston, Massachusetts, USA.
Mark A McClintock
James J Chou
William M Shih

Funding

Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI SANDERS, CHARLES R · 2010 to 2014
$11.5M
NMR Structure Determination of Membrane Proteins Enabled by DNA NanotubesDP2OD004641 · OD · DANA-FARBER CANCER INST · PI SHIH, WILLIAM M · 2008 to 2008
$2.6M
NIGMS NIH HHS U54 GM094608NIH HHS DP2 OD004641
6 · The paper itself

Abstract

Finding a way to determine the structures of integral membrane proteins using solution nuclear magnetic resonance (NMR) spectroscopy has proved to be challenging. A residual-dipolar-coupling-based refinement approach can be used to resolve the structure of membrane proteins up to 40 kDa in size, but to do this you need a weak-alignment medium that is detergent-resistant and it has thus far been difficult to obtain such a medium suitable for weak alignment of membrane proteins. We describe here a protocol for robust, large-scale synthesis of detergent-resistant DNA nanotubes that can be assembled into dilute liquid crystals for application as weak-alignment media in solution NMR structure determination of membrane proteins in detergent micelles. The DNA nanotubes are heterodimers of 400-nm-long six-helix bundles, each self-assembled from a M13-based p7308 scaffold strand and >170 short oligonucleotide staple strands. Compatibility with proteins bearing considerable positive charge as well as modulation of molecular alignment, toward collection of linearly independent restraints, can be introduced by reducing the negative charge of DNA nanotubes using counter ions and small DNA-binding molecules. This detergent-resistant liquid-crystal medium offers a number of properties conducive for membrane protein alignment, including high-yield production, thermal stability, buffer compatibility and structural programmability. Production of sufficient nanotubes for four or five NMR experiments can be completed in 1 week by a single individual.

Indexed as

DetergentsDNAMembrane ProteinsMicellesNanotubesNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryDetergentsDNAMembrane ProteinsMicelles

Identifiers

PMID23518667
PMCPMC3843643

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.