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Related Concept Videos

Protein Folding01:25

Protein Folding

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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
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Chemical and Solubility Equilibria02:21

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The free energy change associated with dissolving a solute in a liter of solvent is called the free energy of a solution, ΔGsolution. The overall ΔGsolution is expressed as the balance of ΔGinteraction against the always-favorable free-energy of mixing, ΔGmixing. Solution formation is favorable if  ΔGsolution is less than zero, whereas it is unfavorable if ΔGsolution is greater than zero. In short, for a solution to form and complete dissolution to take place,...
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Peptide Bonds02:43

Peptide Bonds

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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...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Energetics of Solution Formation02:35

Energetics of Solution Formation

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The formation of a solution is an example of a spontaneous process, which is a process that occurs under specified conditions without energy from some external source.
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Related Experiment Video

Updated: Mar 27, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
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Trace Solvent as a Predominant Factor To Tune Dipeptide Self-Assembly.

Juan Wang, Kai Liu1, Linyin Yan

  • 1University of Chinese Academy of Sciences , Beijing 100049, People's Republic of China.

ACS Nano
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PubMed
Summary

Trace solvents, like water, are crucial for peptide self-assembly. Solvent-bridged hydrogen bonds direct dipeptide fiber formation, highlighting water

Keywords:
dipeptidefibershydrogen bondingself-assemblytrace solvent

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Area of Science:

  • Biomolecular self-assembly
  • Supramolecular chemistry
  • Nanomaterials science

Background:

  • Solvent molecules play a critical role in biological self-assembly processes.
  • Understanding the influence of trace solvents on biomolecular interactions, particularly peptides, is challenging.
  • Noncovalent interactions are key to controlling self-assembly but are difficult to probe at low solvent concentrations.

Purpose of the Study:

  • To investigate the dominant role of trace solvents in mediating dipeptide self-assembly.
  • To identify and demonstrate the specific noncovalent interactions responsible for directing self-assembly.
  • To elucidate the mechanism by which solvents influence the formation of ordered nanostructures.

Main Methods:

  • Utilized hydrogen-bond-forming solvents (ethanol, N,N-dimethylformamide, acetone) to study their effect on diphenylalanine (FF) self-assembly.
  • Analyzed the impact of solvents on hydrogen bonding (C═O and N-H) within FF molecules.
  • Observed the formation of nanofibers and nanobelts through directional hydrogen bonding and long-range ordering.

Main Results:

  • Trace amounts of hydrogen-bond-forming solvents significantly mediate dipeptide self-assembly.
  • Solvent-bridged hydrogen bonding is identified as a crucial force directing the formation of FF nanofibers and nanobelts.
  • Water, a strong hydrogen-bond-forming solvent, accelerates the formation of ordered structures, emphasizing its importance in robust fiber formation.

Conclusions:

  • Trace solvents, particularly those capable of strong hydrogen bonding, are dominant regulators of dipeptide self-assembly.
  • Solvent-bridged hydrogen bonds are essential for achieving directional, one-dimensional self-assembly into nanofibers.
  • Water's role as a trace solvent is critical for the rapid and robust formation of ordered peptide nanostructures.