Jove
Visualize
Contact Us

Related Concept Videos

Protein Folding01:25

Protein Folding

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...
Protein Folding01:22

Protein Folding

Overview
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Polymer Classification: Crystallinity01:21

Polymer Classification: Crystallinity

Unlike ionic or small covalent molecules, polymers do not form crystalline solids due to the diffusion limitations of their long-chain structures. However, polymers contain microscopic crystalline domains separated by amorphous domains.
Crystalline domains are the regions where polymer chains are aligned in an orderly manner and held together in proximity by intermolecular forces. For example, chains in the crystalline domains of polyethylene and nylon are bound together by van der Waals...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Classification and Mechanical Properties of Synthetic Polymers01:28

Classification and Mechanical Properties of Synthetic Polymers

Synthetic polymers are classified as elastomers, fibers, or plastics based on their crystallinity. Crystallinity, the degree of long-range order in the solid state, influences the mechanical properties (stretching or contracting) of elastomers. Elastomers are flexible polymers that can expand or contract easily upon the application of an external force. They have numerous crosslinks that pull them back into their original shape when stress is removed. Silicones, for instance, are highly elastic...

You might also read

Related Articles

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

Sort by
Same author

Perioperative Management: HeartMate 3 Left Ventricular Assist Devices in Non-Cardiac Surgery.

Journal of cardiothoracic and vascular anesthesia·2026
Same author

Optimisation of direct-acting oral anticoagulants (DOACs) use for atrial fibrillation (AF) and venous thromboembolism: a practical guide.

Expert opinion on pharmacotherapy·2026
Same author

Hospitalizations during the 30-day period preceding admission with pulmonary embolism: insights from the National Readmission Database.

Hospital practice (1995)·2025
Same author

The dimensionality of recognition memory: A state-trace analysis of the effects of dividing attention.

Journal of experimental psychology. Learning, memory, and cognition·2025
Same author

Symmetric and asymmetric ligands for Fe<sup>III</sup> spin crossover - the influence of the <i>C</i><sub>2</sub> axis.

Dalton transactions (Cambridge, England : 2003)·2025
Same author

Digital Versus Manual PD-L1 Scoring in Advanced NSCLC From the IMpower110 and IMpower150 Trials.

Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer·2025
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 Video

Updated: Jun 29, 2026

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

Conformational changes and molecular mobility in plasticized proteins.

Ahmad I Athamneh1, Michael Griffin, Meocha Whaley

  • 1Biological Systems Engineering Department, Virginia Tech, 303 Seitz Hall, Blacksburg, Virginia 24061, USA.

Biomacromolecules
|October 14, 2008
PubMed
Summary
This summary is machine-generated.

Biopolymer plasticization depends on molecular structure, not just weight. Glycerol plasticization reveals protein conformational changes influencing material properties from glassy to rubbery states.

More Related Videos

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

Related Experiment Videos

Last Updated: Jun 29, 2026

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
04:37

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

Area of Science:

  • Biochemistry
  • Materials Science
  • Polymer Chemistry

Background:

  • Biopolymers are often plasticized to achieve flexibility, using agents like water or glycerol.
  • The degree of plasticization is influenced by factors beyond molecular weight, including higher-order structures.

Purpose of the Study:

  • To investigate the relationship between protein structure and plasticization extent.
  • To correlate protein conformational changes with material properties under varying plasticization levels.

Main Methods:

  • Proteins (Lactalbumin, ovalbumin, corn zein, wheat gluten, feather keratin) were plasticized with glycerol.
  • Fourier transform-infrared (FT-IR) spectroscopy and X-ray powder diffraction (XRD) monitored protein conformation.
  • Tensile modulus was measured to assess material properties.

Main Results:

  • Plasticization extent is dependent on molecular and higher-order structures.
  • Conformational changes were pronounced in polar proteins with low cysteine content.
  • FT-IR and XRD indicated protein ordering at low to moderate plasticization levels.
  • Glass transition behavior was observed and correlated with modulus, FT-IR, and XRD data.

Conclusions:

  • Protein structure significantly impacts plasticization behavior and resulting material properties.
  • Understanding the glassy-to-rubbery transition is crucial for comparing plasticized biopolymers.
  • FT-IR and XRD are valuable tools for characterizing plasticized biopolymer systems.