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Related Concept Videos

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...

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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

Structural properties of small semiconductor-binding synthetic peptides.

Gökhan Gökoğlu1, Michael Bachmann, Tarik Celik

  • 1Institut für Theoretische Physik, Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany. ggokoglu@hacettepe.edu.tr

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|December 13, 2006
PubMed
Summary

Exhaustive simulations reveal thermodynamic and structural properties of synthetic peptides. These studies characterize helix-coil transitions using a realistic atomic model and implicit solvation.

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Published on: November 21, 2013

Area of Science:

  • Computational chemistry
  • Biophysics
  • Molecular dynamics

Background:

  • Understanding peptide behavior is crucial for drug design.
  • Simulating peptide conformational changes requires advanced computational methods.

Purpose of the Study:

  • To investigate thermodynamic and structural properties of synthetic peptides.
  • To characterize helix-coil transitions in these peptides.

Main Methods:

  • Exhaustive multicanonical Monte Carlo simulations.
  • Realistic all-atom interaction model.
  • Implicit-solvent model for solvation effects.

Main Results:

  • Detailed thermodynamic profiles of peptide folding.
  • Structural analysis revealing key conformational states.
  • Identification of transition points for helix-coil formation.

Conclusions:

  • The study provides insights into peptide folding thermodynamics.
  • Simulations accurately capture helix-coil transitions.
  • The employed model is effective for studying peptide behavior.