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Updated: Jul 7, 2026

A Non-invasive Way to Isolate and Phenotype Cells from the Conjunctiva

A Non-invasive Way to Isolate and Phenotype Cells from the Conjunctiva

Published on: July 5, 2017

Mapping the cytochrome C folding landscape.

Julia G Lyubovitsky¹, Harry B Gray, Jay R Winkler

¹Beckman Institute, California Institute of Technology, Pasadena, California 91125, USA.

Journal of the American Chemical Society

|May 9, 2002

Summary

This summary is machine-generated.

Researchers mapped the protein folding energy landscape of yeast iso-1 cytochrome c using fluorescence energy transfer. They identified distinct collapsed and extended polypeptide populations that rapidly search for the native structure.

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Area of Science:

Biochemistry
Biophysics
Molecular Biology

Background:

Protein folding is a fundamental process governed by the conformational energy landscape.
Understanding this landscape is crucial for deciphering protein structure and function.

Purpose of the Study:

To map the folding energy landscape of Saccharomyces cerevisiae iso-1 cytochrome c.
To investigate the dynamics of protein folding intermediates.

Main Methods:

Utilized fluorescence energy transfer (FRET) kinetics to monitor folding.
Measured the distance between a C-terminal fluorophore and the heme group during folding.
Analyzed protein populations at different folding stages.

Main Results:

Identified two distinct, rapidly equilibrating populations within 1 ms of refolding: collapsed structures (average distance 27 Å) and extended polypeptides (>50 Å).
Native fold formation occurred on a timescale of approximately 300 ms, regulated by heme ligation.
The folding landscape features a narrow central funnel with a flat upper rim facilitating rapid interconversion of intermediates.

Conclusions:

The folding pathway of cytochrome c involves rapid equilibration between collapsed and extended states.
Heme ligation plays a critical role in the final stages of protein folding.
The experimentally determined landscape provides insights into the mechanism of protein folding.