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Related Concept Videos

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.
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Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Molecular Chaperones and Protein Folding03:00

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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...
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Basic Equation for Pressure Field01:13

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The basic equation for a pressure field in fluid mechanics captures the balance of forces within any segment of fluid, providing a foundational understanding of how pressure changes within fluids under various forces. Generally, two main types of forces act on any part of a fluid: surface forces and body forces. Surface forces arise from pressure differences across points within the fluid, which result in net forces that can vary depending on the local pressure gradient. Body forces, on the...

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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

Exploring the folding energy landscape with pressure.

Kazuyuki Akasaka1, Ryo Kitahara, Yuji O Kamatari

  • 1High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan. akasaka@waka.kindai.ac.jp

Archives of Biochemistry and Biophysics
|December 19, 2012
PubMed
Summary

Pressure-controlled nuclear magnetic resonance (NMR) experiments reveal stable protein folding intermediates. This technique provides detailed insights into the protein energy landscape, complementing kinetic studies.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Protein folding is a fundamental process in molecular biology.
  • Understanding the energy landscape of protein folding is crucial for comprehending protein function and dysfunction.
  • Kinetic folding studies often capture transient intermediates, making detailed structural analysis challenging.

Purpose of the Study:

  • To highlight the unique advantages of using pressure as a variable in protein folding studies.
  • To demonstrate how variable-pressure nuclear magnetic resonance (NMR) experiments can stabilize transient protein conformers.
  • To explore the protein energy landscape by examining the conformations of pressure-trapped intermediates.

Main Methods:

  • Conducting variable-pressure NMR experiments under equilibrium conditions.
  • Utilizing high-pressure techniques to stabilize intermediate protein conformations.
  • Applying modern NMR spectroscopy for site-specific conformational analysis of trapped intermediates.

Main Results:

  • Variable-pressure NMR experiments provide unique opportunities to explore the protein folding energy landscape.
  • Pressure can stabilize transient intermediate conformers, enabling their detailed structural examination.
  • The study illustrates the interplay between kinetic and equilibrium pressure-based folding experiments using ubiquitin and hen lysozyme.

Conclusions:

  • Pressure is a powerful tool for dissecting the complex pathways of protein folding.
  • Equilibrium pressure experiments, combined with NMR, offer a complementary approach to kinetic studies for characterizing folding intermediates.
  • This methodology allows for a more comprehensive understanding of protein conformational dynamics and stability.