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Related Concept Videos

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
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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Related Experiment Video

Updated: May 9, 2026

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

Testing the diffusing boundary model for the helix-coil transition in peptides.

Sabine Neumaier1, Andreas Reiner, Maren Büttner

  • 1Munich Center for Integrated Protein Science and Department of Chemistry, Technische Universität München, D-85747 Garching, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|July 24, 2013
PubMed
Summary
This summary is machine-generated.

Peptide helix dynamics are governed by boundary diffusion, a 1D process. Helix unfolding can also occur via coil nucleation, and stabilizing motifs slow boundary diffusion.

Keywords:
-valueprotein foldingα-helix capping

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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

Published on: November 21, 2017

Area of Science:

  • Biophysics
  • Chemical Kinetics

Background:

  • Peptide alpha-helix dynamics and their kinetic mechanisms have been debated.
  • Recent experiments suggest helix-coil dynamics involve boundary movement along the peptide chain.

Purpose of the Study:

  • To test the diffusing boundary model for helix-coil dynamics in peptides of varying lengths.
  • To investigate the influence of amino acid replacements on helix dynamics.

Main Methods:

  • Triplet-triplet energy transfer measurements.
  • Simulations using a kinetic linear Ising model.
  • Analysis of local and nonlocal effects of amino acid substitutions.

Main Results:

  • Boundary diffusion follows a classical 1D Einstein-type process (D = 2.7e7 aa^2/s).
  • Coil nucleation contributes to unfolding in helices longer than 40 amino acids.
  • Helix-stabilizing capping motifs reduce boundary diffusion rates.
  • Single amino acid replacements locally affect dynamics (phi_f = 0.35), indicating pre-existing propensities in the transition state.

Conclusions:

  • The diffusing boundary model accurately describes helix-coil dynamics in peptides.
  • Helix unfolding involves both boundary diffusion and coil nucleation for longer helices.
  • Amino acid replacements have local effects on folding/unfolding and nonlocal effects on unfolding, consistent with the diffusing boundary model.