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Transient folding intermediates characterized by protein engineering.

A Matouschek¹, J T Kellis, L Serrano

¹Department of Chemistry, University of Cambridge, UK.

|August 2, 1990

Summary

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Researchers identified a folding intermediate in barnase mutants, revealing how side chain interactions and the hydrophobic core form during protein folding. This study maps the protein folding pathway using kinetic experiments and NMR.

Area of Science:

Biochemistry and Molecular Biology
Protein Folding Dynamics

Background:

Understanding protein folding pathways is crucial for deciphering protein function and misfolding diseases.
Engineered protein mutants offer unique opportunities to dissect folding intermediates and transition states.

Purpose of the Study:

To identify and characterize intermediates in the folding pathway of barnase.
To map the energetic contributions of side chain tertiary interactions during folding.
To elucidate the sequence of events and structural changes during protein folding.

Main Methods:

Utilized kinetic experiments on engineered barnase mutants.
Employed Nuclear Magnetic Resonance (NMR) spectroscopy for structural characterization.
Combined kinetic data with structural information to map folding intermediates.

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Main Results:

Detected a distinct intermediate state on the barnase folding pathway.
Mapped tertiary interactions and their energetics, noting that many interactions are either fully formed or absent in the intermediate.
Observed progressive consolidation of the hydrophobic core during the folding process.

Conclusions:

The study provides a detailed structural characterization of the barnase folding intermediate.
The findings reveal the dynamic sequence of events and energetic landscape governing barnase folding.
Integration of kinetic and NMR data offers a powerful approach for studying protein folding mechanisms.