Evidence map›Paper›PMID 26446575›Full record

ArticleThe journal of physical chemistry. B2015

Transition Dipoles from 1D and 2D Infrared Spectroscopy Help Reveal the Secondary Structures of Proteins: Application to Amyloids.

Emily B Dunkelberger, Maksim Grechko, Martin T Zanni

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
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  13. Increasing Pump-Probe Signal toward Asymptotic Limits.The journal of physical chemistry. B · 2023
    Review
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  18. Tracking Energy Transfer across a Platinum Center.The journal of physical chemistry. A · 2022
    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

3 authors at 1 institution in 1 country.

Emily B DunkelbergerDepartment of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706-1396, United States.
Maksim GrechkoDepartment of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706-1396, United States.
Martin T ZanniDepartment of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706-1396, United States.
University of Wisconsin–Madison · US

Funding

Structural mechanism of diabetic amyloid formationR01DK079895 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI Martin T Zanni · 2008 to 2026
$7.7M
NIDDK NIH HHS DK79895NIDDK NIH HHS R01 DK079895
6 · The paper itself

Abstract

Transition dipoles are an underutilized quantity for probing molecular structures. The transition dipole strengths in an extended system like a protein are modulated by the couplings and thus probe the structures. Here we measure the absolute transition dipole strengths of human and rat amylin in their solution, aggregated, membrane, and micelleular bound forms, using a combination of 1D and 2D infrared spectroscopy. We find that the vibrational modes of amyloid fibers made of human amylin can extend across as many as 12 amino acids, reflecting very ordered β-sheets in the most carefully prepared samples. Rat amylin has FTIR spectra that are nearly identical in solution, micelles, and membranes. We show that the transition dipoles of rat amylin are much larger when bound to micelles and membranes than when in solution, consistent with rat amylin adopting an α-helical structure. We interpret the transition dipole strengths as experimental measurements of the inverse participation ratio often calculated in theoretical studies. The structure of aggregating and membrane-bound proteins can be difficult to identify with existing techniques, especially during kinetics. These results demonstrate how absolute transition dipoles measured via our 1D/2D spectroscopy method can provide important structural information.

Indexed as

AnimalsHumansIslet Amyloid PolypeptideParticle SizeProtein Structure, SecondaryRatsSpectroscopy, Fourier Transform InfraredIslet Amyloid Polypeptide

Identifiers

PMID26446575
PMCPMC5859136
OpenAlexW2464954382

What OpenQuestion holds

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LicenceTDM
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.