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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Protein Glycosylation01:25

Protein Glycosylation

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Updated: Jun 6, 2026

Probing C84-embedded Si Substrate Using Scanning Probe Microscopy and Molecular Dynamics
13:58

Probing C84-embedded Si Substrate Using Scanning Probe Microscopy and Molecular Dynamics

Published on: September 28, 2016

[Oligoglycine surface structures: molecular dynamics simulation].

O A Gus'kova, P G Khalatur, A R Khokhlov

    Bioorganicheskaia Khimiia
    |November 11, 2010
    PubMed
    Summary

    Full-atomic molecular dynamics simulations reveal that diantennary oligoglycines can form polyglycine II structures on graphite surfaces. This confirms previous atomic-force microscopy findings for these peptide monolayers.

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    Published on: August 13, 2020

    Area of Science:

    • Biophysics
    • Materials Science
    • Computational Chemistry

    Context:

    • Investigating peptide adsorption behavior on surfaces is crucial for understanding biomaterial interactions and designing novel functional materials.
    • Diantennary oligoglycines represent a class of peptides with potential applications in surface coatings and biomolecular engineering.
    • Graphite and mica surfaces offer distinct properties for studying molecular adsorption and self-assembly.

    Purpose:

    • To elucidate the adsorption mechanism of diantennary oligoglycines on graphite and mica surfaces using full-atomic molecular dynamics (MD) simulations.
    • To analyze the structural characteristics of the resulting adsorption layers, focusing on peptide secondary structure.
    • To validate the formation of polyglycine II (PGII) structures in deposited monolayers.

    Summary:

    • Full-atomic MD simulations were performed for diantennary oligoglycines adsorbed onto graphite and mica.
    • Peptide secondary structure motifs were analyzed using STRIDE and DSSP, confirming the possibility of polyglycine II (PGII) formation.
    • The simulation results align with prior atomic-force microscopy estimations for PGII structure in diantennary oligoglycine (DAOG) monolayers on graphite.

    Impact:

    • Provides atomic-level insights into peptide-surface interactions, guiding the design of peptide-based materials.
    • Confirms the formation of specific secondary structures (PGII) in oligoglycine monolayers, relevant for self-assembly studies.
    • Advances the understanding of molecular self-assembly on technologically important surfaces like graphite.