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

Elastin is Responsible for Tissue Elasticity01:12

Elastin is Responsible for Tissue Elasticity

3.3K
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...
3.3K
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.3K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.3K
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

3.5K
Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult...
3.5K
Protein Folding01:25

Protein Folding

11.9K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.9K
Protein Folding01:22

Protein Folding

129.0K
Overview
129.0K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.8K

You might also read

Related Articles

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

Sort by
Same author

pH-dependent surface chemistry and thickness affect the mechanics of hydroxyapatite nanocrystals.

Journal of the mechanical behavior of biomedical materials·2026
Same author

Characterization and development of a gelatin/elastin methacrylamide-based bioink for creating a 3D bioprinted human skin model.

International journal of biological macromolecules·2026
Same author

CD117-Targeted Intraoperative Imaging of Gastrointestinal Stromal Tumor Using a Stem-Cell-Factor-Labeled Fluorophore.

Advanced nanobiomed research·2025
Same author

Influence of Non-Cross-Linking AGEs on Mechanical Properties and Morphological Features of Tropocollagen Peptides: A Molecular Dynamics Study.

ACS biomaterials science & engineering·2025
Same author

A standardized in vitro bioengineered skin for penetrating wound modeling.

In vitro models·2025
Same author

Enhancing drug release from PEG-PLGA implants: The role of Hydrophilic Dexamethasone Phosphate in modulating release kinetics and degradation behavior.

European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences·2025

Related Experiment Video

Updated: Mar 1, 2026

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D
11:46

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D

Published on: May 19, 2018

13.2K

Functions of prolyl hydroxylation in elastin.

Chengeng Yang1, Christian E H Schmelzer2, Anna Tarakanova3

  • 1Department of Biomedical Engineering, University of Connecticut, Storrs, Connecticut, USA.

The Journal of Biological Chemistry
|February 27, 2026
PubMed
Summary

Hydroxyproline modification increases water bonding in elastin, reducing its flexibility. This may protect elastin from degradation and influence tissue assembly, offering insights for biomaterial design.

Keywords:
hydrationhydroxyprolinemolecular dynamicsprolyl hydroxylationprotein dynamicstropoelastin

More Related Videos

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

22.5K
Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
04:30

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

Published on: January 17, 2025

2.2K

Related Experiment Videos

Last Updated: Mar 1, 2026

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D
11:46

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D

Published on: May 19, 2018

13.2K
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

22.5K
Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
04:30

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

Published on: January 17, 2025

2.2K

Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Elastin provides essential tissue elasticity and resilience.
  • Prolyl hydroxylation is an understudied post-translational modification of elastin.
  • Hydroxyproline may alter elastin assembly and resistance to digestion.

Purpose of the Study:

  • To investigate how prolyl hydroxylation affects elastin's protein-solvent interactions and dynamics.
  • To test the hypothesis that hydroxylation modulates elastin behavior.

Main Methods:

  • Molecular dynamics simulations were performed on elastin models with and without prolyl hydroxylation.
  • Analysis focused on hydrogen bonding, configurational space, and protein dynamics.

Main Results:

  • Hydroxyproline increased hydrogen bonding with water by 135% compared to proline.
  • This enhanced hydration reduced local configurational space and negatively impacted elastin's global dynamics.
  • The modification may protect elastin from degradation and influence its assembly.

Conclusions:

  • Prolyl hydroxylation significantly alters elastin's interaction with water, affecting its dynamics.
  • This modification could play a role in elastin's biological functions and resistance to degradation.
  • Findings offer insights for designing engineered elastin-based biomaterials by controlling hydroxyproline content.