Evidence map›Paper›PMID 36520019›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2022

Thermodynamics and Kinetics of a Binary Mechanical System: Mechanisms of Muscle Contraction.

Josh E Baker

Open access · greenAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2022. 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
2.5field-weighted citation impact, top 9% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Scaling in Biological Systems: A Molecular-Ensemble Duality.bioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Four phases of a force transient emerge from a binary mechanical system.Journal of muscle research and cell motility · 2024
    Article
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  5. Article
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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 at 1 institution in 1 country.

Josh E BakerDepartment of Pharmacology, University of Nevada, School of Medicine, Reno, Nevada89557United States.ORCID 0000-0002-2101-5215
University of Nevada, Reno · US

Funding

A Multi-Scale Study of the Interplay Between Force Generating and Force Sensing MR01HL090938 · NHLBI · UNIVERSITY OF NEVADA RENO · PI BAKER, JONATHAN E. · 2008 to 2011
$1.3M
NHLBI NIH HHS R01 HL090938
6 · The paper itself

Abstract

Biological motors function at the interface of biology, physics, and chemistry, and it remains unsettled what rules from which disciplines account for how these motors work. Myosin motors are enzymes that catalyze the hydrolysis of ATP through a mechanism involving a switch-like myosin structural change (a lever arm rotation) induced by actin binding that generates a small displacement of an actin filament. In muscle, individual myosin motors are widely assumed to function as molecular machines having mechanical properties that resemble those of muscle. In a fundamental departure from this perspective, here, I show that muscle more closely resembles a heat engine with mechanical properties that emerge from the thermodynamics of a myosin motor ensemble. The transformative impact of thermodynamics on our understanding of how a heat engine works guides a parallel transformation in our understanding of how muscle works. I consider the simplest possible model of force generation: a binary mechanical system. I develop the mechanics, energetics, and kinetics of this system and show that a single binding reaction generates force when muscle is held at a fixed length and performs work when muscle is allowed to shorten. This creates a network of thermodynamic binding pathways that resembles many of the characteristic mechanical and energetic behaviors of muscle including the muscle force-velocity relationship, heat output by shortening muscle, four phases of a muscle tension transient, spontaneous oscillatory contractions, and force redevelopment. Analogous to the thermodynamic (Carnot) cycle for a heat engine, isothermal and adiabatic binding and detachment reactions create a thermodynamic cycle for muscle that resembles cardiac pressure-volume loops (i.e., how the heart works). This paper provides an outline for how to re-interpret muscle mechanic data using thermodynamics - an ongoing effort that will continue providing novel insights into how muscle and molecular motors work.

Indexed as

Muscle ContractionMyosinsActinsKineticsPhysicsThermodynamicsActinsMyosins

Identifiers

PMID36520019
PMCPMC9798825
OpenAlexW4311578565

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.