Evidence map›Paper›PMID 24341684›Full record

ArticleJournal of the American Chemical Society2014

Crowding induced collective hydration of biological macromolecules over extended distances.

John T King, Evan J Arthur, Charles L Brooks, Kevin J Kubarych

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

46 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Role of Aqueous Media in Macromolecular Crowding.Sub-cellular biochemistry · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Cross-Correlated Motions in Azidolysozyme.Molecules (Basel, Switzerland) · 2022
    Article
  16. Article
  17. Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021
    Review
  18. Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  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

4 authors at 1 institution in 1 country.

John T KingDepartment of Chemistry, University of Michigan , 930 N. University Ave., Ann Arbor, Michigan 48109, United States.
Evan J Arthur
Charles L Brooks
Kevin J Kubarych
University of Michigan–Ann Arbor · US

Funding

WEB BASED DOCUMENTATION &TUTORIALS FOR YAMMPP41RR012255 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROOKS, CHARLES L · 1997 to 2009
$10.4M
NCRR NIH HHS P41 RR012255NCRR NIH HHS RR012255
6 · The paper itself

Abstract

Ultrafast two-dimensional infrared (2D-IR) spectroscopy reveals picosecond protein and hydration dynamics of crowded hen egg white lysozyme (HEWL) labeled with a metal-carbonyl vibrational probe covalently attached to a solvent accessible His residue. HEWL is systematically crowded alternatively with polyethylene glycol (PEG) or excess lysozyme in order to distinguish the chemically inert polymer from the complex electrostatic profile of the protein crowder. The results are threefold: (1) A sharp dynamical jamming-like transition is observed in the picosecond protein and hydration dynamics that is attributed to an independent-to-collective hydration transition induced by macromolecular crowding that slows the hydration dynamics up to an order of magnitude relative to bulk water. (2) The interprotein distance at which the transition occurs suggests collective hydration of proteins over distances of 30-40 Å. (3) Comparing the crowding effects of PEG400 to our previously reported experiments using glycerol exposes fundamental differences between small and macromolecular crowding agents.

Indexed as

Molecular Dynamics SimulationCrystallography, X-RayEgg ProteinsInfrared RaysModels, MolecularProteinsWaterEgg ProteinsProteinsWater

Identifiers

PMID24341684
PMCPMC3983708
OpenAlexW1986985958

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.