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 Concept Videos

Conformity01:20

Conformity

47.9K
Conformity is the change in a person’s behavior to go along with the group, even if that person does not agree with the group.
47.9K
Peptide Bonds02:43

Peptide Bonds

82.6K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
82.6K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.7K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.7K
Conformations of Butane02:20

Conformations of Butane

17.8K
Unlike ethane and propane that have only two major conformations, butane has more than two conformers. The staggered form of butane in which the bulky methyl groups on the two carbons are placed on opposite sides, that is, at a dihedral angle of 180°, is the lowest energy, most stable form — called the anti conformer. This conformation is stabilized due to the absence of steric repulsion between the largely spaced out methyl groups. The other two staggered conformations are...
17.8K
Elastin is Responsible for Tissue Elasticity01:12

Elastin is Responsible for Tissue Elasticity

3.1K
Elastic fiber contains the protein elastin along with lesser amounts of other proteins and glycoproteins. The main property of elastin is that it will return to its original shape after being stretched or compressed. Elastic fibers are prominent in elastic tissues found in skin and the elastic ligaments of the vertebral column.
Ligaments and tendons are made of dense regular connective tissue, but in ligaments not all fibers are parallel. Dense regular elastic tissue contains elastin fibers and...
3.1K
Conformations of Cycloalkanes02:29

Conformations of Cycloalkanes

14.2K
Adolf von Baeyer attempted to explain the instabilities of small and large cycloalkane rings using the concept of angle strain — the strain caused by the deviation of bond angles from the ideal 109.5° tetrahedral value for sp3  hybridized carbons. However, while cyclopropane and cyclobutane are strained, as expected from their highly compressed bond angles, cyclopentane is more strained than predicted, and cyclohexane is virtually strain-free. Hence, Baeyer’s theory that...
14.2K

You might also read

Related Articles

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

Sort by
Same author

Accurate <sup>19</sup>F NMR chemical shifts in Fe(II) complexes with the LH20t local hybrid functional.

Physical chemistry chemical physics : PCCP·2026
Same author

Combined <i>operando</i> UV/vis and NMR spectroscopy gives mechanistic insight into the reaction of guaiazulene with 2,4-dinitrobenzaldehyde.

Physical chemistry chemical physics : PCCP·2026
Same author

A Highly Versatile Enantiodifferentiating Polyglutamate Alignment Medium to Measure Residual Dipolar Couplings in Non-Polar and Polar Solvents.

Journal of the American Chemical Society·2025
Same author

Alternating Orthogonal Switching in a Thiophenyl-Phenyl-Bis-Azobenzene Switch.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

Spin me right round - a versatile BTA-based alignment media toolbox for enhanced enantiodiscrimination.

Chemical communications (Cambridge, England)·2025
Same author

Highly active iron catalysts for olefin hydrogenation enable <i>para</i>-hydrogen induced hyperpolarisation of <sup>1</sup>H and <sup>19</sup>F NMR resonances at 1.4 Tesla.

Chemical communications (Cambridge, England)·2025

Related Experiment Video

Updated: Jan 25, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
07:35

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

Published on: June 9, 2014

22.4K

Temperature induced conformational changes in the elastin-like peptide GVG(VPGVG)3.

Alexander Matt1, Björn Kuttich, Isabelle Grillo

  • 1Institut für Festkörperphysik, Technische Universität Darmstadt, Hochschulstraße 6, 64289 Darmstadt, Germany. b.kuttich@fkp.physik.tu-darmstadt.de.

Soft Matter
|May 9, 2019
PubMed
Summary

Elastin-like peptides undergo conformational changes and aggregation with increasing temperature. This study used small angle neutron scattering to observe these structural shifts in a specific peptide, revealing temperature-dependent aggregate growth.

More Related Videos

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

11.2K
Spatial Separation of Molecular Conformers and Clusters
10:37

Spatial Separation of Molecular Conformers and Clusters

Published on: January 9, 2014

11.7K

Related Experiment Videos

Last Updated: Jan 25, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
07:35

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

Published on: June 9, 2014

22.4K
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

11.2K
Spatial Separation of Molecular Conformers and Clusters
10:37

Spatial Separation of Molecular Conformers and Clusters

Published on: January 9, 2014

11.7K

Area of Science:

  • Biophysics
  • Polymer Science
  • Materials Science

Background:

  • Elastin-like peptides (ELPs) are biopolymers exhibiting Lower Critical Solution Temperature (LCST) behavior.
  • Their solution properties resemble synthetic polymers like polyethylene oxide.
  • Understanding ELP structural transitions is crucial for biomaterial applications.

Purpose of the Study:

  • To investigate the temperature-dependent structural changes of the elastin-like peptide GVG(VPGVG)3.
  • To characterize the conformational changes and aggregation behavior of the peptide.
  • To correlate structural changes with Inverse Temperature Transition (ITT) phenomena.

Main Methods:

  • Small angle neutron scattering (SANS) was employed to study the peptide structure.
  • Experiments were conducted across a temperature range of 25 °C to 70 °C.
  • Scattered intensity and aggregate size were analyzed as a function of temperature and concentration.

Main Results:

  • The peptide's molecular conformation is consistent with a random coil model at lower temperatures.
  • Increasing temperature induced significant conformational changes and peptide aggregation.
  • Aggregate size increased with both temperature and peptide concentration.
  • At low concentrations, temperature-dependent size variation suggested a link to conformational collapse at the ITT.

Conclusions:

  • Elastin-like peptides exhibit complex structural responses to temperature, involving both conformational changes and aggregation.
  • SANS is effective in characterizing these transitions and aggregate formation.
  • The findings provide insights into the behavior of ELPs near their inverse temperature transition.