Evidence map›Paper›PMID 25808204›Full record

ArticleProtein science : a publication of the Protein Society2015

Arginine: Its pKa value revisited.

Carolyn A Fitch, Gerald Platzer, Mark Okon, Bertrand E Garcia-Moreno, Lawrence P McIntosh

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.

0numbers the graph read from it
0cells of the map it votes in
153citing 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

153 citing papers in PubMed.

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  13. HomozygousFrontiers in cardiovascular medicine · 2026
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  19. Cationic Peptoids for Systemic In Vivo Cartilage-Targeting.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  20. Article

93 more citing papers are in PubMed but not listed here.

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.

Carolyn A FitchDepartment of Biophysics, Johns Hopkins University, Baltimore, Maryland, 21218.
Gerald Platzer
Mark Okon
Bertrand E Garcia-Moreno
Lawrence P McIntosh

Funding

Structure-Energy Correlation in ProteinsR01GM061597 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GARCIA-MORENO, BERTRAND · 2001 to 2015
$4.4M
NIGMS NIH HHS GM-061597NIGMS NIH HHS R01 GM061597
6 · The paper itself

Abstract

Using complementary approaches of potentiometry and NMR spectroscopy, we have determined that the equilibrium acid dissociation constant (pKa value) of the arginine guanidinium group is 13.8 ± 0.1. This is substantially higher than that of ∼ 12 often used in structure-based electrostatics calculations and cited in biochemistry textbooks. The revised intrinsic pKa value helps explains why arginine side chains in proteins are always predominantly charged, even at pH values as great as 10. The high pKa value also reinforces the observation that arginine side chains are invariably protonated under physiological conditions of near neutral pH. This occurs even when the guanidinium moiety is buried in a hydrophobic micro-environment, such as that inside a protein or a lipid membrane, thought to be incompatible with the presence of a charged group.

Indexed as

AcidsArginineBinding SitesHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsKineticsLipid BilayersMagnetic Resonance SpectroscopyProteinsAcidsArginineLipid BilayersProteinsequilibrium acid dissociation constantguanidiniumNMR spectroscopypH titrationpKa valuepotentiometryprotein electrostaticstautomer

Identifiers

PMID25808204
PMCPMC4420524

What OpenQuestion holds

Textmetadata
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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.