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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
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
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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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Collapse transition in proteins.

Guy Ziv1, D Thirumalai, Gilad Haran

  • 1Chemical Physics Department, Weizmann Institute of Science, 76100, Rehovot, Israel.

Physical Chemistry Chemical Physics : PCCP
|December 17, 2008
PubMed
Summary
This summary is machine-generated.

The coil-globule transition, crucial for polymer physics, is key to understanding protein folding. Research explores denatured-state collapse using single-molecule fluorescence, revealing insights into protein folding dynamics.

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Area of Science:

  • Polymer Physics
  • Biophysics
  • Protein Folding Dynamics

Background:

  • The coil-globule transition, a fundamental concept in polymer physics, is increasingly recognized as vital for understanding the initial stages of protein folding.
  • Proteins undergo complex conformational changes during folding, with the denatured state's properties significantly influencing the process.

Purpose of the Study:

  • To elucidate the basics of the collapse transition in both homopolymers and proteins.
  • To present studies on denatured-state collapse under equilibrium conditions.
  • To explore the dynamics of protein collapse, both theoretically and experimentally.

Main Methods:

  • Review of the coil-globule transition principles for homopolymers and proteins.
  • Analysis of equilibrium studies on denatured-state collapse.
  • Emphasis on single-molecule fluorescence experiments for denatured state characterization.
  • Theoretical and experimental investigations into collapse dynamics.

Main Results:

  • Characterization of the collapse transition in polymers and proteins.
  • Insights into denatured-state collapse thermodynamics using equilibrium studies.
  • Demonstration of single-molecule fluorescence utility for studying protein denatured states.
  • Limited success in determining the precise rate of collapse, with only an upper limit established.

Conclusions:

  • The coil-globule transition is a critical, yet unresolved, aspect of early protein folding.
  • Single-molecule fluorescence experiments provide valuable data on protein denatured states.
  • Further advancements in experimental and theoretical methods are needed to fully understand the role of denatured-state thermodynamics and dynamics in protein folding.