Evidence map›Paper›PMID 21344534›Full record

ArticleProtein science : a publication of the Protein Society2011

Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.

Mei Hong, Yongchao Su

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
8.8field-weighted citation impact, top 1% of its field
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

46 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Magnetic Alignment of Polymer Nanodiscs Probed by Solid-State NMR Spectroscopy.Langmuir : the ACS journal of surfaces and colloids · 2020
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Towards the Native Binding Modes of Antibiotics that Target Lipid II.Chembiochem : a European journal of chemical biology · 2019
    Review
  12. Article
  13. Determining Cholesterol Binding to Membrane Proteins by CholesterolJournal of the American Chemical Society · 2018
    Article
  14. Review
  15. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Dynamic allostery governs cyclophilin A-HIV capsid interplay.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

2 authors at 1 institution in 1 country.

Mei HongDepartment of Chemistry, Iowa State University, Ames, Iowa 50011, USA. mhong@iastate.edu
Yongchao Su
Iowa State University · US

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
NIGMS NIH HHS R01 GM066976
6 · The paper itself

Abstract

Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the lipid membrane, we have used solid-state NMR spectroscopy to determine the membrane-bound topology of these peptides. A versatile array of solid-state NMR experiments now readily yields the conformation, dynamics, orientation, depth of insertion, and site-specific protein-lipid interactions of these molecules. We summarize key findings of several Arg-rich membrane peptides, including β-sheet antimicrobial peptides, unstructured cell-penetrating peptides, and the voltage-sensing helix of voltage-gated potassium channels. Our results indicate the central role of guanidinium-phosphate and guanidinium-water interactions in dictating the structural topology of these cationic molecules in the lipid membrane, which in turn account for the mechanisms of this functionally diverse class of membrane peptides.

Indexed as

alpha-DefensinsAmino Acid SequenceAnimalsAntimicrobial Cationic PeptidesCationsCell-Penetrating PeptidesDNA-Binding ProteinsHumansLipid BilayersMagnetic Resonance SpectroscopyMembrane ProteinsModels, MolecularMolecular Sequence DataPeptidesPeptides, CyclicPotassium Channels, Voltage-Gatedalpha-DefensinsAntimicrobial Cationic PeptidesCationsCell-Penetrating PeptidesDNA-Binding Proteinshuman neutrophil peptide 1Lipid BilayersMembrane ProteinsPeptidesPeptides, CyclicPotassium Channels, Voltage-Gatedprotegrin-1tachyplesin peptide, Tachypleus tridentatus

Identifiers

PMID21344534
PMCPMC3081543
OpenAlexW2147674336

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.