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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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

Overview
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.

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Related Experiment Video

Updated: Jul 18, 2026

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
13:37

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

Published on: June 20, 2014

Tilted peptides: the history.

Annick Thomas1, Robert Brasseur

  • 1Centre de Biophysique Moléculaire Numérique, FSAGx, Passage des déportés, 2, 5030 Belgium.

Current Protein & Peptide Science
|December 16, 2006
PubMed
Summary

Tilted peptides are novel 2D motifs identified by hydrophobicity, not sequence. These motifs play key roles in virus fusion, protein secretion, and protein structure destabilization, impacting amyloid formation.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Proteins utilize sequence motifs for function, but 2D motifs also exist, detectable in 3D structure.
  • Tilted peptides are a 2D motif characterized by hydrophobicity, not sequence consensus.
  • The first tilted peptide was identified in viral fusion proteins in the 1980s via molecular modeling.

Purpose of the Study:

  • To elucidate the nature and function of tilted peptides as a novel class of protein motifs.
  • To explore the role of tilted peptides in biological processes such as viral fusion and protein secretion.
  • To investigate the potential involvement of tilted peptides in protein structure destabilization and amyloidogenesis.

Main Methods:

  • Deciphering tilted peptides from viral fusion protein sequences using molecular modeling.

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

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Last Updated: Jul 18, 2026

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
13:37

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

Published on: June 20, 2014

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

Published on: November 21, 2013

  • Analyzing the asymmetric hydrophobicity distribution within tilted peptides.
  • Investigating the functional implications of tilted peptides in membrane interactions and protein dynamics.

    • Main Results:

    • Tilted peptides exhibit an asymmetric hydrophobicity distribution, dictating their orientation relative to membranes.
    • These motifs are crucial for viral fusion mechanisms and protein secretion pathways.
    • Tilted peptides are implicated in destabilizing 3D protein structures and driving alpha-to-beta transconformations.

    Conclusions:

    • Tilted peptides represent a significant class of 2D structural motifs with critical biological functions.
    • Their unique hydrophobicity-driven mechanism influences membrane interactions and protein conformational changes.
    • Understanding tilted peptides offers insights into viral mechanisms, protein secretion, and the etiology of amyloid diseases.