Evidence map›Paper›PMID 25060334›Full record

ArticleThe journal of physical chemistry. B2014

Origins of structural flexibility in protein-based supramolecular polymers revealed by DEER spectroscopy.

Nathan A Tavenor, K Ishara Silva, Sunil Saxena, W Seth Horne

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 14% 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

3 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
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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 at 1 institution in 1 country.

Nathan A TavenorDepartment of Chemistry, University of Pittsburgh , Pittsburgh, Pennsylvania 15260, United States.
K Ishara Silva
Sunil Saxena
W Seth Horne
University of Pittsburgh · US

Funding

Acquisition of a High Frequency Pulsed Electron Spin Resonance SpectrometerS10RR028701 · NCRR · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SAXENA, SUNIL K · 2011 to 2011
$1.6M
NCRR NIH HHS S10 RR028701
6 · The paper itself

Abstract

Modular assembly of bio-inspired supramolecular polymers is a powerful technique to develop new soft nanomaterials, and protein folding is a versatile basis for preparing such materials. Previous work demonstrated a significant difference in the physical properties of closely related supramolecular polymers composed of building blocks in which identical coiled-coil-forming peptides are cross-linked by one of two subtly different organic linkers (one flexible and the other rigid). Herein, we investigate the molecular basis for this observation by isolating a single subunit of the supramolecular polymer chain and probing its structure and conformational flexibility by double electron-electron resonance (DEER) spectroscopy. Experimental spin-spin distance distributions for two different labeling sites coupled with molecular dynamics simulations provide insights into how the linker structure impacts chain dynamics in the coiled-coil supramolecular polymer.

Indexed as

Electron Spin Resonance SpectroscopyAmino Acid SequenceCircular DichroismCrystallography, X-RayMolecular Dynamics SimulationMolecular Sequence DataPeptidesPolymersProtein Structure, SecondarySpin LabelsPeptidesPolymersSpin Labels

Identifiers

PMID25060334
PMCPMC4141697
OpenAlexW2012216818

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.