Evidence map›Paper›PMID 23062349›Full record

ArticleBiophysical journal2012

Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.

Jonathan D Nickels, Hugh O'Neill, Liang Hong, Madhusudan Tyagi, Georg Ehlers, Kevin L Weiss, Qiu Zhang, Zheng Yi, Eugene Mamontov, Jeremy C Smith and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 149 citations in OpenAlex.

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  13. Water in protein hydration and ligand recognition.Journal of molecular recognition : JMR · 2019
    Review
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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

11 authors at 3 institutions in 1 country.

Jonathan D NickelsJoint Institute for Neutron Sciences, Oak Ridge National Laboratory, Oak Ridge, TN, USA.
Hugh O'Neill
Liang Hong
Madhusudan Tyagi
Georg Ehlers
Kevin L Weiss
Qiu Zhang
Zheng Yi
Eugene Mamontov
Jeremy C Smith
Alexei P Sokolov
Oak Ridge National Laboratory · USUniversity of Tennessee at Knoxville · USNational Institute of Standards and Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present a detailed analysis of the picosecond-to-nanosecond motions of green fluorescent protein (GFP) and its hydration water using neutron scattering spectroscopy and hydrogen/deuterium contrast. The analysis reveals that hydration water suppresses protein motions at lower temperatures (<~ 200 K), and facilitates protein dynamics at high temperatures. Experimental data demonstrate that the hydration water is harmonic at temperatures <~ 180-190 K and is not affected by the proteins' methyl group rotations. The dynamics of the hydration water exhibits changes at ~ 180-190 K that we ascribe to the glass transition in the hydrated protein. Our results confirm significant differences in the dynamics of protein and its hydration water at high temperatures: on the picosecond-to-nanosecond timescale, the hydration water exhibits diffusive dynamics, while the protein motions are localized to <~3 Å. The diffusion of the GFP hydration water is similar to the behavior of hydration water previously observed for other proteins. Comparison with other globular proteins (e.g., lysozyme) reveals that on the timescale of 1 ns and at equivalent hydration level, GFP dynamics (mean-square displacements and quasielastic intensity) are of much smaller amplitude. Moreover, the suppression of the protein dynamics by the hydration water at low temperatures appears to be stronger in GFP than in other globular proteins. We ascribe this observation to the barrellike structure of GFP.

Indexed as

Neutron DiffractionDeuteriumGreen Fluorescent ProteinsModels, MolecularProtein Structure, SecondaryTemperatureWaterDeuteriumGreen Fluorescent ProteinsWater

Identifiers

PMID23062349
PMCPMC3471459
OpenAlexW1980469312

What OpenQuestion holds

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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.