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Related Concept Videos

Protein Folding01:22

Protein Folding

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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.
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Protein Organization01:24

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Mechanisms of Membrane Domain Formation00:59

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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Published on: February 6, 2020

Foldamer structuring by covalently bound macromolecules.

Koushik Ghosh1, Jeffrey S Moore

  • 1Department of Chemistry and the Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

Journal of the American Chemical Society
|November 17, 2011
PubMed
Summary
This summary is machine-generated.

Large macromolecules attached to meta-phenylene ethynylene (mPE) foldamers induce them to collapse into a helical structure. This folding effect is more pronounced with larger macromolecules, offering insights into intrinsically unstructured proteins.

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Last Updated: May 27, 2026

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07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Area of Science:

  • Polymer Chemistry
  • Biophysics
  • Macromolecular Science

Background:

  • Intrinsically unstructured proteins (IUPs) play crucial roles in cellular environments by interacting with and influencing other proteins.
  • Foldamers are synthetic polymers designed to adopt specific conformations, serving as models for biological macromolecules.

Purpose of the Study:

  • To investigate the effect of attached macromolecules on the conformational folding of meta-phenylene ethynylene (mPE) oligomers.
  • To explore the molecular weight dependence of macromolecule-induced folding in mPE foldamers.
  • To establish mPE foldamers as model systems for studying the physics of IUPs.

Main Methods:

  • Fluorescence spectroscopy was employed to monitor conformational changes.
  • Electronic absorption spectroscopy was used to analyze the electronic properties related to conformation.
  • Experiments were conducted on mPE dodecamers with varying sizes of attached macromolecules.

Main Results:

  • Macromolecules attached to both ends of the mPE dodecamer induced collapse into a presumed helical conformation.
  • The folding effect was significantly enhanced when macromolecule segments exceeded approximately 50 kDa.
  • Conformational structuring was observed even in denaturing solvents for sufficiently large attached macromolecules.

Conclusions:

  • Chain-centered foldamers can be induced to fold by external macromolecules, mimicking aspects of IUP behavior.
  • The size of the inducing macromolecule is a critical factor in the extent of foldamer collapse.
  • These findings support the utility of foldamers as model systems for fundamental research on intrinsically unstructured proteins.