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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
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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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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
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Probing the cytochrome c' folding landscape.

Ekaterina V Pletneva1, Ziqing Zhao, Tetsunari Kimura

  • 1Beckman Institute, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, USA.

Journal of Inorganic Biochemistry
|August 4, 2007
PubMed
Summary

The folding of Rhodospirillum palustris cytochrome c

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Area of Science:

  • Biochemistry
  • Protein Folding
  • Spectroscopy

Background:

  • Cytochrome c' (cyt c') from Rhodospirillum palustris is crucial for electron transfer.
  • Understanding protein folding kinetics is essential for molecular biology.
  • Cytochrome c' folding presents unique challenges due to its heme group and complex structure.

Purpose of the Study:

  • To investigate the folding kinetics of R. palustris cytochrome c' at pH 5.
  • To identify intermediate states and rate-limiting steps during folding.
  • To explore the role of prolyl isomerase in cytochrome c' folding.

Main Methods:

  • Monitoring folding using heme absorption and tryptophan fluorescence.
  • Analyzing transient absorption spectra to detect kinetic deviations.
  • Utilizing cyclophilin as a prolyl isomerase to assess its effect on folding.

Main Results:

  • Trp72 fluorescence indicated early polypeptide compaction.
  • Heme transient absorption revealed deviations from two-state folding, including a slow phase.
  • Cyclophilin accelerated the slow folding phase, suggesting a role in proline isomerization.

Conclusions:

  • The folding of R. palustris cytochrome c' is complex, not a simple two-state process.
  • A nonnative proline configuration (Pro21) likely hinders helical bundle formation.
  • Prolyl isomerase (cyclophilin) can facilitate the resolution of proline-related folding intermediates.