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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Bibliographic Details
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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Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1016/S0022-2836(02)00441-2