Polymer Folding
Polymer Folding - Related Videos
08:12
Depolymerizable Olefinic Polymers Based on Fused-Ring Cyclooctene Monomers
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2022
Here, we describe protocols for the preparation of trans-cyclobutane fused cyclooctenes (tCBCO), their polymerization to prepare depolymerizable olefinic polymers, and the depolymerization of these polymers under mild conditions. Additionally, protocols for the preparation of depolymerizable networks and compression molding of rigid linear plastics based on this system are described.
03:00
Molecular Chaperones and Protein Folding
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2020
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...
01:49
Protein Folding
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2020
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation which is 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 FunctionProteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:49
Protein Folding
0 Views •
2026
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation which is 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 FunctionProteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11:11
Construction and Characterization of a Novel Vocal Fold Bioreactor
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Cited by 8 •
2014
A novel vocal fold bioreactor capable of delivering physiologically relevant, vibratory stimulation to cultured cells is constructed and characterized. This dynamic culture device, when combined with a fibrous poly(ε-caprolactone) scaffold, creates a vocal fold-mimetic environment that modulates the behaviors of mesenchymal stem cells.
FAQs
Hydrophobic effects, hydrogen bonding, electrostatic forces, and steric constraints jointly shape the accessible conformations. Interactions within the chain favor some contacts, while the surrounding solvent changes which contacts are energetically favorable. Their balance determines whether a chain settles into a compact, ordered arrangement or another accessible state, making solvent conditions important when interpreting folding behavior.
The energy landscape represents the range of conformations available to a chain and the energetic preferences separating them. Folding can guide the polymer toward one or more favored states, but the pathway is not always fully equilibrated. Kinetic trapping may preserve intermediate structures, so the observed conformation can reflect both stability and the route taken.
Several conformations may have similar energetic advantages because different intrachain contacts and solvent interactions can be favorable at the same time. The resulting states may differ in three-dimensional organization, stability, or accessibility without requiring a single universal structure. Recognizing multiple favored states helps explain conformational variability and supports more realistic interpretations of polymer behavior.
Sequence establishes the chemical features and potential interaction patterns along the chain, whereas the environment influences how those features interact. Changes in solvent conditions can therefore alter the balance among hydrophobic, hydrogen-bonding, electrostatic, and steric effects. Relating sequence to environmental context allows researchers to connect molecular design with stability, structure, and function.
A conceptual design workflow begins by relating polymer sequence and environmental conditions to favored conformations, stability, and kinetics. Bioengineers can then consider how those structural outcomes affect function or material behavior. This approach supports the design of proteins, nucleic-acid structures, responsive biomaterials, and drug-delivery systems while accounting for both stable states and trapped intermediates.
Folding analysis can connect molecular conformation with stability, assembly, mechanical behavior, and biological function. It helps researchers ask whether a chosen sequence and environment favor the intended structural state or produce alternative intermediates. These relationships are useful for interpreting why a designed polymer performs as expected, changes its behavior, or fails to reach a desired configuration.
In bioengineering, folding provides a link between molecular-level interactions and engineered outcomes. Understanding how chains respond to sequence and solvent conditions can guide the development of functional proteins, nucleic-acid architectures, responsive materials, and delivery systems. It also helps researchers anticipate how conformational stability and kinetics may influence assembly, mechanical properties, and biological activity.