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ArticleDoklady. Biochemistry and biophysics2021

Temperature Dependence of Tryptophan Fluorescence Lifetime as an Indicator of Its Microenvironment Dynamics.

V V Gorokhov, B N Korvatovsky, P P Knox, N P Grishanova, S N Goryachev, V Z Pashchenko, A B Rubin

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Article in Doklady. Biochemistry and biophysics, 2021. 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
–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

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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.

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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

7 authors.

V V GorokhovMoscow State University, Moscow, Russia. Gorokhgiceron149@gmail.com.
B N KorvatovskyMoscow State University, Moscow, Russia.
P P KnoxMoscow State University, Moscow, Russia.
N P GrishanovaMoscow State University, Moscow, Russia.
S N GoryachevMoscow State University, Moscow, Russia.
V Z PashchenkoMoscow State University, Moscow, Russia.
A B RubinMoscow State University, Moscow, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spectral-kinetic characteristics of the fluorescence of the tryptophan molecule in an aqueous solution and in the composition of a protein (albumin) were studied in the temperature range from -170 to 25°C. To explain the observed changes in the spectra and the tryptophan fluorescence lifetime with temperature, a model of transitions between the excited and ground states involving a charge-transfer state was used, which takes into account the nonlinear nature of the dynamics of these transitions. In these processes, an important role is played by the interaction of tryptophan molecules with its microenvironment, as well as rearrangements in the system of hydrogen bonds of the water-protein matrix surrounding the tryptophan molecule.

Indexed as

AnimalsCattleFluorescenceHydrogen BondingKineticsSerum Albumin, BovineSpectrometry, FluorescenceTemperatureTryptophanWaterSerum Albumin, BovineTryptophanWaterfluorescencehydrogen bondsmolecular dynamicstryptophan

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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.