Evidence map›Paper›PMID 26477255›Full record

ArticleMethods in enzymology2015

Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy.

Lishan Liu, Daniel J Mayo, Indra D Sahu, Andy Zhou, Rongfu Zhang, Robert M McCarrick, Gary A Lorigan

Abstract read
In one paragraph

Article in Methods in enzymology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 4% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Angewandte Chemie (International ed. in English) · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Utilization ofBiochimica et biophysica acta. Biomembranes · 2018
    Article
  10. Review
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

7 authors at 1 institution in 1 country.

Lishan LiuDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA. Electronic address: lorigag@miamioh.edu.
Daniel J MayoDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
Indra D SahuDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
Andy ZhouDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
Rongfu ZhangDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
Robert M McCarrickDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
Gary A LoriganDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.
Miami University · US

Funding

EPR Structural Studies of KCNE1/KCNQ1R01GM108026 · NIGMS · MIAMI UNIVERSITY OXFORD · PI LORIGAN, GARY A · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM108026
6 · The paper itself

Abstract

Revealing detailed structural and dynamic information of membrane embedded or associated proteins is challenging due to their hydrophobic nature which makes NMR and X-ray crystallographic studies challenging or impossible. Electron paramagnetic resonance (EPR) has emerged as a powerful technique to provide essential structural and dynamic information for membrane proteins with no size limitations in membrane systems which mimic their natural lipid bilayer environment. Therefore, tremendous efforts have been devoted toward the development and application of EPR spectroscopic techniques to study the structure of biological systems such as membrane proteins and peptides. This chapter introduces a novel approach established and developed in the Lorigan lab to investigate membrane protein and peptide local secondary structures utilizing the pulsed EPR technique electron spin echo envelope modulation (ESEEM) spectroscopy. Detailed sample preparation strategies in model membrane protein systems and the experimental setup are described. Also, the ability of this approach to identify local secondary structure of membrane proteins and peptides with unprecedented efficiency is demonstrated in model systems. Finally, applications and further developments of this ESEEM approach for probing larger size membrane proteins produced by overexpression systems are discussed.

Indexed as

Amino Acid SequenceAnimalsElectron Spin Resonance SpectroscopyHumansMembrane ProteinsMolecular Sequence DataPeptidesProtein Structure, SecondarySpin LabelsMembrane ProteinsPeptidesSpin LabelsESEEMMembrane peptideMembrane proteinPulsed EPRSDSLSecondary structure

Identifiers

PMID26477255
PMCPMC4814931
OpenAlexW1827503608

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.