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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
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...
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...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Polypeptide chain collapse and protein folding.

Jayant B Udgaonkar1

  • 1National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India. jayant@ncbs.res.in

Archives of Biochemistry and Biophysics
|October 23, 2012
PubMed
Summary

Polypeptide chain collapse is crucial for protein folding. This review scrutinizes how chain collapse interacts with secondary structure, hydrophobic core consolidation, and tertiary interactions, referencing key folding models.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein folding is essential for cellular function.
  • Polypeptide chain collapse is a key early event in protein folding.
  • Understanding folding mechanisms is critical for protein engineering and disease research.

Purpose of the Study:

  • To review and scrutinize the experimental characterization of polypeptide chain collapse.
  • To examine the interplay between chain collapse and other folding events like secondary structure formation and hydrophobic core development.
  • To analyze the polypeptide chain collapse reaction within the framework of established protein folding models.

Main Methods:

  • Literature review of experimental studies on protein folding.
  • Analysis of experimental data characterizing polypeptide chain collapse.
  • Comparison of experimental findings with theoretical models of protein folding.

Main Results:

  • Polypeptide chain collapse is integral to secondary and tertiary structure formation.
  • The timing and nature of chain collapse influence the folding pathway.
  • Experimental evidence supports various aspects of different folding models.

Conclusions:

  • Chain collapse is a fundamental process that drives protein folding.
  • The interplay between collapse and other folding events dictates the final protein structure.
  • Further experimental validation is needed to fully elucidate the role of chain collapse in different folding models.