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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.
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
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...
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...
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...

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Updated: Jun 24, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Structural determinants of protein folding.

Tse Siang Kang1, R Manjunatha Kini

  • 1The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Cellular and Molecular Life Sciences : CMLS
|April 16, 2009
PubMed
Summary

Structural biology advances enable rapid protein structure determination. This review explores key structural determinants driving protein folding, a fundamental biochemical challenge.

Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Recent decades show significant advances in spectroscopic techniques, molecular biology, and computational power.
  • These advancements have accelerated the elucidation of biomacromolecule structures.
  • Despite progress, protein folding remains a fundamental challenge in biochemistry.

Purpose of the Study:

  • To review identified structural determinants of protein folding.
  • To explore the driving forces behind polypeptide chain conformation.

Main Methods:

  • Review of recent decades' findings in structural biology.
  • Analysis of spectroscopic, molecular biology, and computational techniques.
  • Examination of empirical data on protein folding.

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

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12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

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Last Updated: Jun 24, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Main Results:

  • Advances in techniques have increased the rate of protein structure determination.
  • Specific structural determinants influencing protein folding have been identified.
  • Understanding these determinants is crucial for solving the protein folding puzzle.

Conclusions:

  • Continued research into structural determinants is essential for advancing protein folding knowledge.
  • Elucidating these forces aids in understanding protein function and disease.
  • Interdisciplinary approaches combining biology, chemistry, and computation are key.