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Protein Folding

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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.
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Synthesis of an Intein-mediated Artificial Protein Hydrogel

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

Mutual synergistic protein folding in split intein.

Yuchuan Zheng¹, Qin Wu, Chunyu Wang

¹CAS Key Laboratory of Soft Matter Chemistry, Department of Chemistry, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.

Bioscience Reports

|June 12, 2012

Summary

Split inteins, like DnaE from Synechocystis, associate via robust thermodynamic interactions. This protein association is essential for initiating the trans-splicing activity required for protein ligation.

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Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Area of Science:

Protein biochemistry
Molecular biology
Structural biology

Background:

Inteins are protein sequences that excise themselves and ligate flanking protein sequences.
Split inteins are expressed as two separate fragments, requiring association for function.
The DnaE split intein from Synechocystis sp. PCC6803 is a model system for studying split intein mechanisms.

Purpose of the Study:

To investigate the structural and thermodynamic basis of the interaction between the two halves of the Synechocystis DnaE split intein.
To understand how the association of split intein fragments leads to functional complex formation.

Main Methods:

Structural analysis of split intein fragments.
Thermodynamic analysis using isothermal titration calorimetry (ITC).
Conformational analysis of isolated and associated intein halves.

Main Results:

The isolated DnaE split intein halves (IN and IC) are intrinsically disordered.
Association of the IN and IC halves induces a disorder-to-order conformational transition.
Isothermal titration calorimetry demonstrated that a favorable enthalpy change drives the association, outweighing unfavorable entropy changes.
High flexibility and strong thermodynamic preference ensure robust association and formation of a well-folded IN/IC complex.

Conclusions:

The robust association of DnaE split intein halves is driven by favorable enthalpy changes, overcoming entropic penalties.
The conformational transition from disorder to order upon association is critical for forming the functional split intein complex.
This study provides insights into the molecular mechanisms underlying split intein-mediated protein trans-splicing.