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Equilibrium Folding and Stability of Myotrophin: A Model Ankyrin Repeat Protein

Proteins containing stretches of repeating amino acid sequences are prevalent throughout nature, yet little is known about the general folding and assembly mechanisms of these systems. Here we propose myotrophin as a model system to study the folding of ankyrin repeat proteins. Myotrophin is folded...

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Published in:	Journal of molecular biology 2002-07, Vol.320 (2), p.165-170
Main Authors:	Mosavi, Leila K., Williams, Suzanna, Peng, Zheng-yu
Format:	Article
Language:	English
Subjects:	Animals Ankyrin Repeat Circular Dichroism Dose-Response Relationship, Drug Growth Substances - chemistry Hydrogen-Ion Concentration Intercellular Signaling Peptides and Proteins internal repeat sequences Kinetics Magnetic Resonance Spectroscopy myotrophin Protein Denaturation Protein Folding Rats stability Temperature Thermodynamics two-state folding Urea - pharmacology
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container_title	Journal of molecular biology
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creator	Mosavi, Leila K. Williams, Suzanna Peng, Zheng-yu
description	Proteins containing stretches of repeating amino acid sequences are prevalent throughout nature, yet little is known about the general folding and assembly mechanisms of these systems. Here we propose myotrophin as a model system to study the folding of ankyrin repeat proteins. Myotrophin is folded over a large pH range and is soluble at high concentrations. Thermal and urea denaturation studies show that the protein displays cooperative two-state folding properties despite its modular nature. Taken together with previous studies on other ankyrin repeat proteins, our data suggest that the two-state folding pathway may be characteristic of ankyrin repeat proteins and other integrated α-helical repeat proteins in general.
doi_str_mv	10.1016/S0022-2836(02)00441-2
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subjects	Animals Ankyrin Repeat Circular Dichroism Dose-Response Relationship, Drug Growth Substances - chemistry Hydrogen-Ion Concentration Intercellular Signaling Peptides and Proteins internal repeat sequences Kinetics Magnetic Resonance Spectroscopy myotrophin Protein Denaturation Protein Folding Rats stability Temperature Thermodynamics two-state folding Urea - pharmacology
title	Equilibrium Folding and Stability of Myotrophin: A Model Ankyrin Repeat Protein
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