Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Elastin: a representative ideal protein elastomer.

D W Urry1, T Hugel, M Seitz

  • 1University of Minnesota, Twin Cities Campus, BioTechnology Institute, 1479 Gortner Avenue, St Paul, MN 55108-6106, USA. durry98@aol.com

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|March 26, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Expression of an environmentally friendly synthetic protein-based polymer gene in transgenic tobacco plants.

Plant cell reports·2013
Same author

Probing surfaces with single-polymer atomic force microscope experiments.

Biointerphases·2010
Same author

Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected].

The Review of scientific instruments·2009
Same author

Painted supported lipid membranes.

Biophysical journal·2009
Same author

Imaging viscoelasticity by force modulation with the atomic force microscope.

Biophysical journal·2009
Same author

Single-molecule cut-and-paste surface assembly.

Science (New York, N.Y.)·2008
Same journal

The microlandscapes of tree trunks: the effect of lichen and tree-level characteristics on arthropod communities.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2026
Same journal

Centimetre-scale landscapes to assess the motion behaviour and cognition of gastropods and bivalves.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2026
Same journal

Intertidal microcosms of wave-swept rocky shores: ecological and physiological insights from a uniquely stressful environment.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2026
Same journal

Temporal and spatial variation in temperature and oxygen at the microscale: key niche axes for aquatic life.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2026
Same journal

Natural microcosms in ecology: fulfilling the promise of model systems?

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2026
Same journal

Microbe-induced galls and plant defence: metabolite crosstalk in a co-evolutionary battle.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences·2026
See all related articles

Protein elastomers, like elastin, exhibit ideal elasticity not from random chains, but from dynamic, non-random structures. These structures provide entropic elasticity by damping internal chain dynamics during extension.

Area of Science:

  • Biophysics
  • Materials Science
  • Polymer Chemistry

Background:

  • Traditionally, ideal protein elastomers were believed to require a random chain network structure.
  • Elastin, the protein in mammalian elastic fibers, is a key example of a biological elastomer.

Purpose of the Study:

  • To investigate the structural basis of ideal elasticity in protein elastomers.
  • To challenge the prevailing theory that random chain networks are necessary for entropic elasticity.

Main Methods:

  • Atomic force microscopy (AFM) to obtain single-chain force-extension curves.
  • Low-frequency sound absorption measurements.
  • Review of previous data including dielectric relaxation, thermoelasticity, and molecular dynamics simulations.

Related Experiment Videos

Main Results:

  • Single-chain force-extension curves of (GVGVP)(251) and (GVGIP)(260) provide evidence for single-chain ideal elasticity.
  • Elastin-based polymers show distinct sound absorption properties compared to random-chain elastomers.
  • Data supports the presence of dynamic, non-random structural elements in elastin.

Conclusions:

  • Elastin and its components possess regularly repeating, non-random structures that contribute to its elastic properties.
  • These structures exhibit predominantly entropic elasticity through the damping of internal chain dynamics upon extension.
  • The findings challenge the long-held view that random chain networks are essential for ideal protein elastomers.