Evidence map›Paper›PMID 29498890›Full record

ReviewAnnual review of biophysics2018

Structure and Dynamics of Membrane Proteins from Solid-State NMR.

Venkata S Mandala, Jonathan K Williams, Mei Hong

Abstract readReview
In one paragraph

Review in Annual review of biophysics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

64 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Homonuclear Simplified Preservation of Equivalent Pathways Spectroscopy.The journal of physical chemistry letters · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Diamond rotors.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
  18. Article
  19. Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers.Journal of the American Chemical Society · 2023
    Article
  20. Great Offset Difference Internuclear Selective Transfer.The journal of physical chemistry letters · 2023
    Article

4 more citing papers are in PubMed but not listed here.

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

3 authors.

Venkata S MandalaDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: meihong@mit.edu.
Jonathan K WilliamsDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: meihong@mit.edu.
Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; email: meihong@mit.edu.

Funding

Structures and lipid interactions of curvature-inducing membrane peptides by NMRR01GM066976 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2003 to 2021
$4.8M
Structures and Dynamics of Proton and Cation-Dependent Channels and TransportersR01GM088204 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2009 to 2024
$4.8M
NIGMS NIH HHS R01 GM066976NIGMS NIH HHS R01 GM088204
6 · The paper itself

Abstract

Solid-state nuclear magnetic resonance (SSNMR) spectroscopy elucidates membrane protein structures and dynamics in atomic detail to yield mechanistic insights. By interrogating membrane proteins in phospholipid bilayers that closely resemble biological membranes, SSNMR spectroscopists have revealed ion conduction mechanisms, substrate transport dynamics, and oligomeric interfaces of seven-transmembrane helix proteins. Research has also identified conformational plasticity underlying virus-cell membrane fusions by complex protein machineries, and β-sheet folding and assembly by amyloidogenic proteins bound to lipid membranes. These studies collectively show that membrane proteins exhibit extensive structural plasticity to carry out their functions. Because of the inherent dependence of NMR frequencies on molecular orientations and the sensitivity of NMR frequencies to dynamical processes on timescales from nanoseconds to seconds, SSNMR spectroscopy is ideally suited to elucidate such structural plasticity, local and global conformational dynamics, protein-lipid and protein-ligand interactions, and protonation states of polar residues. New sensitivity-enhancement techniques, resolution enhancement by ultrahigh magnetic fields, and the advent of 3D and 4D correlation NMR techniques are increasingly aiding these mechanistically important structural studies.

Indexed as

HumansMembrane ProteinsNuclear Magnetic Resonance, BiomolecularMembrane Proteinsconformational dynamicsion channelsmagic-angle-spinning NMRtransportersviral fusion proteins

Identifiers

PMID29498890
PMCPMC6312106

What OpenQuestion holds

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Registered trials

None linked

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.