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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...
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...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
piRNA - Piwi-interacting RNAs02:57

piRNA - Piwi-interacting RNAs

PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while only 2000 genes have been found for miRNAs. piRNAs can act at the transcriptional and post-transcriptional levels and have a vital role in silencing transposable elements present in germ cells. They are also involved in epigenetic silencing and activation. Previously, they were thought to function only in germ cells but new evidence suggests...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

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Updated: Jun 11, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

n-->pi* interactions in proteins.

Gail J Bartlett1, Amit Choudhary, Ronald T Raines

  • 1School of Chemistry, University of Bristol, Bristol, United Kingdom.

Nature Chemical Biology
|July 13, 2010
PubMed
Summary
This summary is machine-generated.

Protein backbone amides engage in n-->pi* interactions, a key interaction beyond hydrogen bonds. These significant interactions are prevalent in protein secondary structures, influencing protein folding and stability.

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Hydrogen bonds are widely recognized as crucial for stabilizing protein structures.
  • The role of other interactions, such as electronic effects between backbone amide and carbonyl groups, is less understood.

Purpose of the Study:

  • To investigate the prevalence and significance of n-->pi* interactions in protein structures.
  • To explore the impact of these interactions on protein folding, stability, and function.

Main Methods:

  • Utilized Natural Bond Orbital (NBO) analysis to predict n-->pi* interactions.
  • Performed statistical analysis on a high-resolution protein structure dataset to validate predictions.
  • Examined the occurrence of n-->pi* interactions in various protein secondary structures.

Main Results:

  • NBO analysis identified significant n-->pi* interactions in specific regions of the Ramachandran plot.
  • Statistical analysis confirmed the prevalence of these interactions in high-resolution protein structures.
  • n-->pi* interactions were found to be abundant in alpha-helices, 3(10)-helices, polyproline II helices, and twisted beta-sheets.

Conclusions:

  • n-->pi* interactions represent an important, yet often overlooked, force in protein structure stabilization.
  • These interactions play a significant role in protein folding and function.
  • The findings suggest that n-->pi* interactions should be incorporated into computational force fields for more accurate protein modeling.