Evidence map›Paper›PMID 30763085›Full record

ArticleThe journal of physical chemistry. B2019

Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering.

Dolev Rimmerman, Denis Leshchev, Darren J Hsu, Jiyun Hong, Baxter Abraham, Robert Henning, Irina Kosheleva, Lin X Chen

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Temporal ghost imaging for pump-probe X-ray solution scattering.Acta crystallographica. Section A, Foundations and advances · 2025
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  11. Time-resolved X-ray scattering studies of proteins.Current opinion in structural biology · 2021
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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

8 authors at 3 institutions in 1 country.

Dolev RimmermanDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.ORCID 0000-0002-9957-2839
Denis LeshchevDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.
Darren J HsuDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.
Jiyun HongDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.
Baxter AbrahamDepartment of Chemistry and Biochemistry , University of Delaware , Newark , Delaware 19716 , United States.
Robert HenningCenter for Advanced Radiation Sources , The University of Chicago , Chicago , Illinois 60637 , United States.
Irina KoshelevaCenter for Advanced Radiation Sources , The University of Chicago , Chicago , Illinois 60637 , United States.
Lin X ChenDepartment of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.ORCID 0000-0002-8450-6687
Northwestern University · USUniversity of Chicago · USUniversity of Delaware · US

Funding

Electric Field-stimulated Protein MechanicsP41GM118217 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH, RANGANATHAN, RAMA · 2019 to 2021
$5.3M
Capturing Transient Protein Structures on Multiple Spatial and Temporal ScalesR01GM115761 · NIGMS · NORTHWESTERN UNIVERSITY · PI CHEN, LIN X · 2015 to 2023
$3.0M
BioCARS: A Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
NIGMS NIH HHS R01 GM115761NIGMS NIH HHS R24 GM111072
6 · The paper itself

Abstract

Many biomaterials can adapt to changes in the local biological environment (such as pH, temperature, or ionic composition) in order to regulate function or deliver a payload. Such adaptation to environmental perturbation is typically a hierarchical process that begins with a response at a local structural level and then propagates to supramolecular and macromolecular scales. Understanding fast structural dynamics that occur upon perturbation is important for rational design of functional biomaterials. However, few nanosecond time-resolved methods can probe both intra- and intermolecular scales simultaneously with a high structural resolution. Here, we utilize time-resolved X-ray scattering to probe nanosecond to microsecond structural dynamics of poly-l-glutamic acid undergoing protonation via a pH jump initiated by photoexcitation of a photoacid. Our results provide insights into the protonation-induced hierarchical changes in packing of peptide chains, formation of a helical structure, and the associated collapse of the peptide chain.

Indexed as

ProtonsHydrogen-Ion ConcentrationPeptidesPolyglutamic AcidProtein Conformation, alpha-HelicalStereoisomerismX-Ray DiffractionPeptidesPolyglutamic AcidProtons

Identifiers

PMID30763085
PMCPMC6533112
OpenAlexW2912903764

What OpenQuestion holds

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LicenceTDM
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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.