Evidence map›Paper›PMID 33951045›Full record

ArticlePloS one2021

Bridging between material properties of proteins and the underlying molecular interactions.

Guang Song

Abstract read
In one paragraph

Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Conducting Atomic Force Microscopy of Protein Wires.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  2. Article
  3. 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

1 author.

Guang SongDepartment of Computer Science, Iowa State University, Ames, IA, United States of America.ORCID 0000-0002-5153-6695

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work, we develop a novel method that bridges between material properties of proteins, particularly the modulus of elasticity, and the underlying molecular interactions. To this end, we employ both an all-atom normal mode analysis (NMA) model with the CHARMM force field and an elastic solid model for proteins and protein interfaces. And the "bridge" between the two models is a common physical property predictable by both models: the magnitude of thermal vibrations. This connection allows one to calibrate the Young's moduli of proteins and protein interface regions. We find that the Young's moduli of proteins are in the range of a few Gpa to 10 Gpa, while the Young's moduli of the interface regions are several times smaller. The work is significant as it represents the first attempt to systematically compute the elastic moduli of proteins from molecular interactions.

Indexed as

Elastic ModulusProteinsElasticityModels, MolecularProteins

Identifiers

PMID33951045
PMCPMC8099097

What OpenQuestion holds

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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.