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Updated: May 27, 2026

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Mutation-induced fold switching among lattice proteins.

Christian Holzgräfe¹, Anders Irbäck, Carl Troein

¹Computational Biology and Biological Physics, Lund University, Sölvegatan 14A, SE-223 62 Lund, Sweden. christian.holzgraefe@thep.lu.se

The Journal of Chemical Physics

|November 25, 2011

Summary

Single mutations can cause proteins to switch folds, but finding these pathways is hard. Our study on a simple model shows these switches are common and minimum-mutation paths miss many real connections.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Published on: May 13, 2020

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Last Updated: May 27, 2026

Microfluidic Mixers for Studying Protein Folding

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Published on: April 10, 2012

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

Computational biology
Protein folding
Biophysics

Background:

Recent experiments identified single mutations causing protein fold switching.
Identifying such mutational pathways in real proteins remains a significant challenge.

Purpose of the Study:

To analyze single-mutation-induced fold switching in a minimalistic hydrophobic/polar model on a square lattice.
To investigate the network topology of fold switches and evaluate search strategies for fold pathways.

Main Methods:

Generation of a comprehensive sequence-structure database for protein chains up to length 30 in a hydrophobic/polar model.
Analysis of single-mutation-induced fold switching events and the resulting fold network topology.
Comparison of different search strategies for identifying fold-switched pairs, including minimum-mutation paths.

Main Results:

Single-mutation-induced fold switching is common in the analyzed model.
The resulting fold network exhibits a topology similar to randomly connected nodes.
A restricted search strategy focusing only on minimum-mutation paths incorrectly identifies 40% of single-mutation-linked fold pairs.
Thermodynamic stability is correlated with mutational stability and is reduced at fold switches.

Conclusions:

Fold switching is a prevalent phenomenon in simplified protein models.
Simple search strategies based on minimum mutations are insufficient for accurately identifying fold-switched protein pairs.
Fold switches are associated with reduced thermodynamic and mutational stability.