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The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ermolenkov, Vladimir V. Fredriksen, Laura Xu, Ming Zagorevski, Dmitri Shashilov, Victor A. Lednev, Igor K.
Description	Country affiliation: United States Author Affiliation: Xu M ( Department of Chemistry, University at Albany, SUNY, Albany, New York 12222, USA.)
Abstract	Amyloid fibril depositions are associated with many neurodegenerative diseases as well as amyloidosis. The detailed molecular mechanism of fibrillation is still far from complete understanding. In our previous study of in vitro fibrillation of hen egg white lysozyme, an irreversible partially unfolded intermediate was characterized. A similarity of unfolding kinetics found for the secondary and tertiary structure of lysozyme using deep UV resonance Raman (DUVRR) and tryptophan fluorescence spectroscopy leads to a hypothesis that the unfolding might be a two-state transition. In this study, chemometric analysis, including abstract factor analysis (AFA), target factor analysis (TFA), evolving factor analysis (EFA), multivariate curve resolution-alternating least squares (ALS), and genetic algorithm, was employed to verify that only two principal components contribute to the DUVRR and fluorescence spectra of soluble fraction of lysozyme during the fibrillation process. However, a definite conclusion on the number of conformers cannot be made based solely on the above spectroscopic data although chemometric analysis suggested the existence of two principal components. Therefore, electrospray ionization mass spectrometry (ESI-MS) was also utilized to address the hypothesis. The protein ion charge state distribution (CSD) envelopes of the incubated lysozyme were well fitted with two principal components. Based on the above analysis, the partial unfolding of lysozyme during in vitro fibrillation was characterized quantitatively and proven to be a two-state transition. The combination of ESI-MS and Raman and fluorescence spectroscopies with advanced statistical analysis was demonstrated to be a powerful methodology for studying protein structural transformations.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	16
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2007-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Muramidase Chemistry Phase Transition Animals Kinetics Models, Statistical Protein Conformation Protein Denaturation Protein Folding Spectrometry, Fluorescence Spectrometry, Mass, Electrospray Ionization Spectrum Analysis, Raman Tryptophan Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition

Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme.

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Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme.

Kinetic traps in lysozyme folding.

Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL).

Role of individual disulfide bonds in hen lysozyme early folding steps.

Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation

Modelling protein unfolding: hen egg-white lysozyme.

The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition.

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The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition

Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme.

Hexafluoroacetone hydrate as a structure modifier in proteins: characterization of a molten globule state of hen egg-white lysozyme.

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The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition.