Evidence map›Paper›PMID 25964322›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Protein aggregation in salt solutions.

Miha Kastelic, Yurij V Kalyuzhnyi, Barbara Hribar-Lee, Ken A Dill, Vojko Vlachy

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
–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

38 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions.International journal of molecular sciences · 2022
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Deciphering Spectroscopic Signatures of Competing CaThe journal of physical chemistry. B · 2024
    Article
  8. Article
  9. Article
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  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Evidence for a semisolid phase state of aerosols and droplets relevant to the airborne and surface survival of pathogens.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021
    Review
  19. Article
  20. 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.

Miha KastelicFaculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia;
Yurij V KalyuzhnyiInstitute for Condensed Matter Physics, 79011 Lviv, Ukraine;
Barbara Hribar-LeeFaculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia;
Ken A DillLaufer Center for Physical and Quantitative Biology and Departments of Physics and Chemistry, Stony Brook University, Stony Brook, NY 11794 dill@laufercenter.org.
Vojko VlachyFaculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia;

Funding

Modeling Aqueous Solvation in BiologyR01GM063592 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DILL, KEN A · 2001 to 2018
$4.3M
Modeling Aqueous Solvation in BiologyR56GM063592 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DILL, KEN A · 2009 to 2009
$330k
NIGMS NIH HHS GM063592NIGMS NIH HHS R01 GM063592NIGMS NIH HHS R56 GM063592
6 · The paper itself

Abstract

Protein aggregation is broadly important in diseases and in formulations of biological drugs. Here, we develop a theoretical model for reversible protein-protein aggregation in salt solutions. We treat proteins as hard spheres having square-well-energy binding sites, using Wertheim's thermodynamic perturbation theory. The necessary condition required for such modeling to be realistic is that proteins in solution during the experiment remain in their compact form. Within this limitation our model gives accurate liquid-liquid coexistence curves for lysozyme and γ IIIa-crystallin solutions in respective buffers. It provides good fits to the cloud-point curves of lysozyme in buffer-salt mixtures as a function of the type and concentration of salt. It than predicts full coexistence curves, osmotic compressibilities, and second virial coefficients under such conditions. This treatment may also be relevant to protein crystallization.

Indexed as

Models, ChemicalProtein AggregatesCrystallizationgamma-CrystallinsMuramidaseOsmosisProteinsSaltsSolutionsSystems BiologyThermodynamicsgamma-CrystallinsMuramidaseProtein AggregatesProteinsSaltsSolutionsHofmeister seriesphase separationprotein aggregation

Identifiers

PMID25964322
PMCPMC4450416

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.