Evidence map›Paper›PMID 32277554›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.

Evan S O'Brien, Brian Fuglestad, Henry J Lessen, Matthew A Stetz, Danny W Lin, Bryan S Marques, Kushol Gupta, Karen G Fleming, A Joshua Wand

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Side-chain dynamics of the αProtein science : a publication of the Protein Society · 2023
    Article
  11. Deep mining of the protein energy landscape.Structural dynamics (Melville, N.Y.) · 2023
    Article
  12. Article
  13. Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Untangling the complexity of membrane protein folding.Current opinion in structural biology · 2022
    Review
  16. Article
  17. Review
  18. Membrane proteins enter the fold.Current opinion in structural biology · 2021
    Review
  19. Article
  20. Structural cavities are critical to balancing stability and activity of a membrane-integral enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

9 authors at 3 institutions in 1 country.

Evan S O'BrienDepartment of Biochemistry & Biophysics, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, 19104, USA.ORCID 0000-0002-2260-7722
Brian FuglestadDepartment of Biochemistry & Biophysics, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, 19104, USA.
Henry J LessenDepartment of Biophysics, Johns Hopkins University, Baltimore, MD, 21218, USA.
Matthew A StetzDepartment of Biochemistry & Biophysics, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, 19104, USA.
Danny W LinDepartment of Biochemistry & Biophysics, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, 19104, USA.
Bryan S MarquesDepartment of Biochemistry & Biophysics, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, 19104, USA.
Kushol GuptaDepartment of Biochemistry & Biophysics, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, 19104, USA.
Karen G FlemingDepartment of Biophysics, Johns Hopkins University, Baltimore, MD, 21218, USA.
A Joshua WandDepartment of Biochemistry & Biophysics, Texas A&M University, College Station, TX, 77843, USA.ORCID 0000-0001-8341-0782
University of Pennsylvania · USJohns Hopkins University · USVirginia Commonwealth University · US

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Membrane Protein StabilityR01GM079440 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FLEMING, KAREN G. · 2009 to 2022
$4.1M
NIGMS NIH HHS P30 GM133893NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM079440NIGMS NIH HHS T32 GM008275NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side-chain dynamics of the α-helical sensory rhodopsin II and the β-barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Despite their differing topologies, both proteins have a similar distribution of methyl-bearing side-chain motion that is largely independent of membrane mimetic. The methyl-bearing side chains of both proteins are, on average, more dynamic in the ps-ns timescale than any soluble protein characterized to date. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect. Furthermore, the high conformational entropy could greatly influence the thermodynamics underlying membrane-protein functions, including ligand binding, allostery, and signaling.

Indexed as

EntropyCrystallography, X-RayMembrane ProteinsMolecular ConformationNuclear Magnetic Resonance, BiomolecularMembrane Proteinsconformational entropymembrane proteinsNMR spectroscopyprotein foldingside-chain dynamics

Identifiers

PMID32277554
PMCPMC7318686
OpenAlexW3016109661

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.