From Globular Proteins to Amyloids

Häftad, Engelska, 2019

Av Roterman-Konieczna,Iren, Irena Roterman-Konieczna, Poland) Roterman-Konieczna, Irena (Professor of Bioinformatics, Jagiellonian University

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From Globular Proteins to Amyloids proposes a model and mechanism for explaining protein misfolding. Concepts presented are based on a model originally intended to show how proteins attain their native conformations. This model is quantitative in nature and founded upon arguments derived from information theory. It facilitates prediction and simulation of the amyloid fibrillation process, also identifying the progressive changes that occur in native proteins that lead to the emergence of amyloid aggregations.

Introduces basic rules for protein folding, along with the conditions that result in misfolding
Presents research that lies in treating the aqueous environment as a continuum rather than a set of individual water molecules (i.e. the classic representation)
Provides practical applications for helping the prevention of amyloidosis and improving drug design

Produktinformation

Utgivningsdatum2019-10-02
Mått152 x 229 x undefined mm
Vikt460 g
FormatHäftad
SpråkEngelska
Antal sidor278
FörlagElsevier Science
ISBN9780081029817

Tillhör följande kategorier

Biokemisk teknik inom Naturvetenskap och teknik
Biokemi inom Naturvetenskap och teknik
Farmakologi inom Medicin

Professor Irena Roterman-Konieczna completed her PhD at the Nicolaus Copernicus Medical Academy Krakow, Poland and undertook her postdoctoral studies at Cornell University, USA. She is the director of the Department of Bioinformatics and Telemedicine at Jagiellonian University – Medical College, Poland. Her fields of interest are protein structure, folding simulation as well as systems biology. She is the author of "Protein Folding in Silico", published by Woodhead Publishing in 2012., and "From Globular Proteins to Amyloids" published by Elsevier in 2020. She is the Chief Editor of the journal Bio-Algorithms and Med-Systems (de Gruyter).

1. Description of the fuzzy oil drop model2. Folding with the active participation of water3. Information coded in protein structure4. Gobular or ribbon-like micelle5. Proteins structured as spherical micelles6. Local discordance6. A. The active site in a single-chain enzyme identified as local deficiency of hydrophobicity6. B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface6. C. Ligand binding cavity coded in form of local deficiency of hydrophobicity7. Solenoid – amyloid under control8. Composite structures9. Permanent chaperons9. A. Non-amyloid structure of the aβ(1-42) polypeptide requiring a permanent chaperone9. B. Structural properties of aβ(1-42) chain fragments in complex with proteins acting as permanent chaperones10. Amyloids10. A. Amyloid as a ribbon-like micelle10. B. Alternative conformations of the aβ(1-40) amyloid protein10. C. Specificity of amino acid sequence and its role in secondary and super secondary structure generation11. Anti-amyloid drug design12. Predicted structure of the transthyretin amyloid