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Calcium-binding lysozymes
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Denver University.
Institute for Biological Instrumentation of the Russian Academy of Sciences.
2012 (English)Book (Other academic)
Abstract [en]

In this book, the authors describe an important class of calcium binding lysozymes that are evolutionarily related to the lysozyme superfamily and the lactalbumins. The authors take the reader through a journey from the evolution, then the structure and properties of the calcium binding lysozymes. They discuss new unique protein folding pathways with local cooperative, close related folding modes that exhibit multiple folding pathways which are not properties of the lactalbumins or non calcium binding lysozymes. They comprise one of the most diverse group of examples in protein folding. In addition this protein class, especially equine lysozyme, shows peculiar amyloid assembly properties that are not common with other fibril forming proteins. It is one of the first shown to form ring shaped amyloids and other complexes in vitro. Lastly equine lysozyme forms complex with oleic acid, a unique form ELOA, which contributes to the family of the human and bovine lactalbumin analogs HAMLET and BAMLET.

Place, publisher, year, edition, pages
New York: Nova Science Publishers, Inc., 2012. , 171 p.
National Category
Cell and Molecular Biology
URN: urn:nbn:se:umu:diva-64172ISBN: 978-1-62081-755-1OAI: diva2:589294
Available from: 2013-01-17 Created: 2013-01-17 Last updated: 2013-09-10Bibliographically approved

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Morozova-Roche, Ludmilla
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