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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
Protein Organization01:13

Protein Organization

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Protein Organization01:24

Protein Organization

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.
The primary structure of a protein is its amino acid sequence.
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...

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Related Experiment Video

Updated: Jul 11, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

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All-cis helical polypeptides.

Romuald Poteau1, Georges Trinquier

  • 1Laboratoire de Physique et Chimie des Nano-Objets (UMR5215, CNRS-UPS-INSA), IRSAMC, Institut National des Sciences Appliquées, 31077 Toulouse Cedex 4, France.

The Journal of Organic Chemistry
|October 6, 2007
PubMed
Summary

Exploring all-cis open-chain polypeptides reveals novel helical structures. Quantum chemistry shows these structures are thermodynamically feasible and kinetically stable, challenging previous assumptions.

Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Structural Biology

Background:

  • All-cis open-chain polypeptides are rarely studied due to scarcity of cis peptide bonds, lower thermodynamic stability of cis amide bonds, and perceived steric clashes.
  • Existing models often overlook the potential for cis isomers in polypeptide structures.

Purpose of the Study:

  • To investigate the feasibility and structural characteristics of all-cis open-chain polypeptides.
  • To address the thermodynamic and steric constraints associated with cis peptide bonds in polypeptide backbones.
  • To explore novel conformational possibilities beyond traditional trans-peptide bond structures.

Main Methods:

  • Quantum-chemistry calculations were performed on alanine tridecamers to model all-cis polypeptide structures.

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  • Analysis involved classical Ramachandran maps (E = f(phi i,psi i)) and novel plaque maps (E = f(phi i,psi i-1)).
  • Characterization of helical arrangements and intramolecular hydrogen bonding.

    • Main Results:

    • Proper phi/psi adjustments in all-cis polypeptides can relieve steric constraints, enabling several helical arrangements.
    • Four distinct helical structures were identified, including a superhelix with intramolecular hydrogen bonds.
    • Assembly of cis-prepared building units is an exothermic process, and the resulting all-cis backbone exhibits kinetic stability.

    Conclusions:

    • All-cis open-chain polypeptides can adopt stable helical structures, challenging the notion of inherent instability.
    • The study introduces plaque maps for analyzing conformational dependence between consecutive residues, impacting understanding of local effects.
    • These findings suggest that all-cis polypeptides possess significant potential for novel biomaterial and drug design.