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Related Concept Videos

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.
Protein Organization01:13

Protein Organization

Overview
Peptide Bonds02:43

Peptide Bonds

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...
Protein Folding01:22

Protein Folding

Overview
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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Related Experiment Video

Updated: Jun 20, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Electron delocalization and charge transfer in polypeptide chains.

Ye-Fei Wang1, Zhang-Yu Yu, Jian Wu

  • 1Institute of Theoretical Chemistry, Shandong University, Jinan 250100 Shandong, China.

The Journal of Physical Chemistry. A
|September 8, 2009
PubMed
Summary
This summary is machine-generated.

Electron delocalization in polypeptide chains favors the amino end due to hyperconjugation and hydrogen bonds. This study suggests a superexchange mechanism for electron transfer in these biological molecules.

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Determination of the Gas-phase Acidities of Oligopeptides
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Determination of the Gas-phase Acidities of Oligopeptides

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Last Updated: Jun 20, 2026

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Determination of the Gas-phase Acidities of Oligopeptides
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Determination of the Gas-phase Acidities of Oligopeptides

Published on: June 24, 2013

Area of Science:

  • Computational chemistry
  • Biophysics
  • Molecular modeling

Background:

  • Polypeptide chains are fundamental biological molecules.
  • Understanding electron structure and charge transfer is crucial for biological processes.

Purpose of the Study:

  • Investigate electron structure and charge-transfer mechanisms in polypeptide chains.
  • Analyze electron delocalization pathways and their directionality.
  • Identify the dominant mechanism for electron transfer.

Main Methods:

  • Natural Bond Orbital (NBO) analysis.
  • Density Functional Theory (DFT) calculations using B3LYP/6-311++G**.
  • Analysis of hyperconjugative interactions and hydrogen bonding.

Main Results:

  • Electron delocalization occurs in both directions between peptide subgroups, with a preference from the carboxyl to the amino end.
  • Strong hyperconjugative interaction involving pi*C-O orbitals facilitates delocalization.
  • Intramolecular hydrogen bonds (O...H-N) further support electron delocalization towards the amino end.

Conclusions:

  • Electron flow in polypeptide chains is directed towards the amino end.
  • The superexchange mechanism is proposed as the primary mode of electron transfer.
  • These findings provide insights into charge transport in biological systems.