Evidence map›Paper›PMID 26266732›Full record

ArticleThe journal of physical chemistry letters2015

Biomolecular Crowding Arising from Small Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement.

Mary Rose Hilaire, Rachel M Abaskharon, Feng Gai

Abstract readLetter
In one paragraph

Article in The journal of physical chemistry letters, 2015. 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. Do guanidinium and tetrapropylammonium ions specifically interact with aromatic amino acid side chains?Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Review
  7. 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.

Mary Rose HilaireDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Rachel M AbaskharonDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Feng GaiDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.

Funding

ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
Spectroscopic Study of Protein Folding DynamicsR01GM065978 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2002 to 2014
$3.9M
NIGMS NIH HHS GM-065978NIGMS NIH HHS P41 GM104605NIGMS NIH HHS P41-GM104605NIGMS NIH HHS R01 GM065978
6 · The paper itself

Abstract

The effect of macromolecular crowding on the structure, dynamics, and reactivity of biomolecules is well established and the relevant research has been extensively reviewed. Herein, we focus our discussion on crowding effects arising from small cosolvent molecules and densely packed surface conditions. In addition, we highlight recent efforts that capitalize on the excluded volume effect for various tailored biochemical and biophysical applications. Specifically, we discuss how a targeted increase in local mass density can be exploited to gain insight into the folding dynamics of the protein of interest and how confinement via reverse micelles can be used to study a range of biophysical questions, from protein hydration dynamics to amyloid formation.

Indexed as

Macromolecular SubstancesModels, MolecularProtein FoldingProteinsThermodynamicsMacromolecular SubstancesProteins

Identifiers

PMID26266732
PMCPMC4610718

What OpenQuestion holds

Textmetadata
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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.