Evidence map›Paper›PMID 16500987›Full record

ArticleBiophysical journal2006

Sub-angstrom conformational changes of a single molecule captured by AFM variance analysis.

Kirstin A Walther, Jasna Brujić, Hongbin Li, Julio M Fernández

Abstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  7. Quantifying DNA melting transitions using single-molecule force spectroscopy.Journal of physics. Condensed matter : an Institute of Physics journal · 2009
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Kirstin A WaltherDepartment of Physics, Columbia University, New York, New York, USA.
Jasna Brujić
Hongbin Li
Julio M Fernández

Funding

Nanomechanics of the extracellular matrixR01HL066030 · NHLBI · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI FERNANDEZ, JULIO M · 2001 to 2013
$5.0M
NHLBI NIH HHS R01 HL066030NHLBI NIH HHS R01 HL66030
6 · The paper itself

Abstract

A system's equilibrium variance can be analyzed to probe its underlying dynamics at higher resolution. Here, using single-molecule atomic-force microscope techniques, we show how the variance in the length of a single dextran molecule can be used to establish thermodynamic equilibrium and to detect conformational changes not directly observable with other methods. Dextran is comprised of a chain of pyranose rings that each undergoes an Angstrom-scale transition from a chair to boat conformation under a stretching force. Our analysis of the variance of the molecule's fluctuations verifies equilibrium throughout the force-extension curve, consistent with the expected thermodynamic ensemble. This validates further analysis of the variance in the transition region, which reveals an intermediate conformation between the chair and the boat on the sub-Angstrom scale. Our test of thermal equilibrium as well as our variance analysis can be readily extended to a wide variety of molecules, including proteins.

Indexed as

Models, ChemicalModels, MolecularAnalysis of VarianceComputer SimulationDextransElasticityMicrochemistryMicroscopy, Atomic ForceMolecular ConformationStress, MechanicalDextrans

Identifiers

PMID16500987
PMCPMC1440761

What OpenQuestion holds

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Registered trials

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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.