Evidence map›Paper›PMID 31054180›Full record

ArticleProtein science : a publication of the Protein Society2019

Controlling and quantifying protein concentration in Escherichia coli.

Shannon L Speer, Alex J Guseman, Jon B Patteson, Brandie M Ehrmann, Gary J Pielak

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2019. 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
0.9field-weighted citation impact, top 28% 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. The intracellular environment affects protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  2. Article
  3. 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

5 authors at 1 institution in 1 country.

Shannon L SpeerDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
Alex J GusemanDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
Jon B PattesonDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
Brandie M EhrmannDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
Gary J PielakDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.ORCID 0000-0001-6307-542X
University of North Carolina at Chapel Hill · US

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
MOLECULAR AND CELLULAR BIOPHYSICS TRAINING PROGRAMT32GM008570 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A, SLEP, KEVIN C · 1995 to 2022
$5.1M
Protein stabilizers from tardigradesR01GM127291 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PIELAK, GARY JOSEPH · 2019 to 2021
$1.4M
NCI NIH HHS P30 CA016086NIGMS NIH HHS R01 GM127291NIGMS NIH HHS T32 GM008570NIH HHS CA016086NIH HHS R01GM127291
6 · The paper itself

Abstract

The cellular environment is dynamic and complex, involving thousands of different macromolecules with total concentrations of hundreds of grams per liter. However, most biochemistry is conducted in dilute buffer where the concentration of macromolecules is less than 10 g/L. High concentrations of macromolecules affect protein stability, function, and protein complex formation, but to understand these phenomena fully we need to know the concentration of the test protein in cells. Here, we quantify the concentration of an overexpressed recombinant protein, a variant of the B1 domain of protein G, in Tuner (DE3)™ Escherichia coli cells as a function of inducer concentration. We find that the protein expression level is controllable, and expression saturates at over 2 mM upon induction with 0.4 mM isopropyl β-d-thiogalactoside. We discuss the results in terms of what can and cannot be learned from in-cell protein NMR studies in E. coli.

Indexed as

Bacterial ProteinsEscherichia coliMacromolecular SubstancesNuclear Magnetic Resonance, BiomolecularProtein DomainsRecombinant ProteinsBacterial ProteinsIgG Fc-binding protein, StreptococcusMacromolecular SubstancesRecombinant ProteinsEscherichia coliflow cytometryin-cell NMRmass spectrometryprotein expression

Identifiers

PMID31054180
PMCPMC6566559
OpenAlexW2943871566

What OpenQuestion holds

Textmetadata
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.