Evidence map›Paper›PMID 41432205›Full record

ArticleFEBS open bio2026

Polarization-resolved femtosecond Vis/IR spectroscopy tailored for resolving weak signals in biological samples using minimal sample volume.

Clark Zahn, Karsten Heyne

Abstract read
In one paragraph

Article in FEBS open bio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

2 authors.

Clark ZahnDepartment of Physics, Free University Berlin, Germany.
Karsten HeyneDepartment of Physics, Free University Berlin, Germany.ORCID https://orcid.org/0000-0002-3243-9160

Funding

Deutsche Forschungsgemeinschaft 169703910Deutsche Forschungsgemeinschaft 490942819Deutsche Forschungsgemeinschaft SFB 1078 project B7
6 · The paper itself

Abstract

Photoreceptor proteins have a variety of functions and properties that are utilized in cells. The starting point is the absorption of light by a chromophore, triggering a cascade of specific reactions in the protein lasting from femtoseconds to seconds. To understand the individual early reaction steps, we need to trace the ultrafast structural dynamics. In this report, we present our approach towards improving the signal-to-noise ratio in polarization-resolved transient infrared (IR) spectroscopy, enabling such measurements. We outline our polarization-resolved ultrafast visible (Vis)-pump/IR-probe spectroscopy setup using IR referencing. The setup is tailored towards tracing small signals of photo-degrading biological samples (e.g. site-specific mutant proteins, that are available only in limited quantities). We provide a comprehensive overview on characterizing the excitation conditions for polarization resolved measurements. The obtained spectra allow for direct tracing of reaction dynamics and conformational changes of molecular groups within the chromophore, protein side chains and hydrogen-bond network.

Indexed as

ProteinsSignal-To-Noise RatioSpectrophotometry, InfraredProteinsanisotropycontinuum bandinfrared spectroscopypolarization resolved spectroscopyultrafast protein dynamicsultrafast spectrocsopy

Identifiers

PMID41432205
PMCPMC13398637

What OpenQuestion holds

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Registered trials

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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.