Evidence map›Paper›PMID 21619030›Full record

ArticleBiochemistry2011

Influence of histidine tag attachment on picosecond protein dynamics.

Megan C Thielges, Jean K Chung, Jun Y Axup, Michael D Fayer

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

23 citing papers in PubMed, 49 citations in OpenAlex.

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  19. Line shape analysis of two-dimensional infrared spectra.The Journal of chemical physics · 2015
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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

4 authors at 2 institutions in 1 country.

Megan C ThielgesDepartment of Chemistry, Stanford University, Stanford, California 94305, USA.
Jean K Chung
Jun Y Axup
Michael D Fayer
Stanford University · USScripps Research Institute · US

Funding

Protein, Enzyme, and Biological Water Dynamics: 2D Vibrational Echo SpectroscopyR01GM061137 · NIGMS · STANFORD UNIVERSITY · PI FAYER, MICHAEL D · 2000 to 2011
$3.1M
Protein Dynamics and Substrate Specificity in Cytochrome P450sF32GM090549 · NIGMS · STANFORD UNIVERSITY · PI THIELGES, MEGAN CORRINE · 2010 to 2012
$120k
NIGMS NIH HHS 2R01-GM061137-09NIGMS NIH HHS F32 GM090549NIGMS NIH HHS F32-GM090549NIGMS NIH HHS R01 GM061137
6 · The paper itself

Abstract

Polyhistidine affinity tags are routinely employed as a convenient means of purifying recombinantly expressed proteins. A tacit assumption is commonly made that His tags have little influence on protein structure and function. Attachment of a His tag to the N-terminus of the robust globular protein myoglobin leads to only minor changes to the electrostatic environment of the heme pocket, as evinced by the nearly unchanged Fourier transform infrared spectrum of CO bound to the heme of His-tagged myoglobin. Experiments employing two-dimensional infrared vibrational echo spectroscopy of the heme-bound CO, however, find that significant changes occur to the short time scale (picoseconds) dynamics of myoglobin as a result of His tag incorporation. The His tag mainly reduces the dynamics on the 1.4 ps time scale and also alters protein motions of myoglobin on the slower, >100 ps time scale, as demonstrated by the His tag's influence on the fluctuations of the CO vibrational frequency, which reports on protein structural dynamics. The results suggest that affinity tags may have effects on protein function and indicate that investigators of affinity-tagged proteins should take this into consideration when investigating the dynamics and other properties of such proteins.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceAnimalsCarbon MonoxideHistidineMolecular Sequence DataMyoglobinProtein BindingRecombinant ProteinsSpectroscopy, Fourier Transform InfraredSperm WhaleStatic ElectricityTime FactorsCarbon MonoxideHistidineMyoglobinpolyhistidineRecombinant Proteins

Identifiers

PMID21619030
PMCPMC3133630
OpenAlexW1989879685

What OpenQuestion holds

Textmetadata
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.