Evidence map›Paper›PMID 21895221›Full record

ArticleThe Journal of chemical physics2011

Electrostatics and aggregation: how charge can turn a crystal into a gel.

Jeremy D Schmit, Stephen Whitelam, Ken Dill

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Growth rates of protein crystals.Journal of the American Chemical Society · 2012
    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

3 authors.

Jeremy D SchmitDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA. schmit@phys.ksu.edu
Stephen Whitelam
Ken Dill

Funding

COMBINATORIAL STATISTICAL MECHANICS OF PROTEIN FOLDINGR01GM034993 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DILL, KEN A · 1985 to 2009
$2.7M
NIGMS NIH HHS GM34993NIGMS NIH HHS R01 GM034993
6 · The paper itself

Abstract

The crystallization of proteins or colloids is often hindered by the appearance of aggregates of low fractal dimension called gels. Here we study the effect of electrostatics upon crystal and gel formation using an analytic model of hard spheres bearing point charges and short range attractive interactions. We find that the chief electrostatic free energy cost of forming assemblies comes from the entropic loss of counterions that render assemblies charge-neutral. Because there exists more accessible volume for these counterions around an open gel than a dense crystal, there exists an electrostatic entropic driving force favoring the gel over the crystal. This driving force increases with increasing sphere charge, but can be counteracted by increasing counterion concentration. We show that these effects cannot be fully captured by pairwise-additive macroion interactions of the kind often used in simulations, and we show where on the phase diagram to go in order to suppress gel formation.

Indexed as

CrystallizationGelsStatic ElectricitySaltsGelsSalts

Identifiers

PMID21895221
PMCPMC3182083

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.