From Globular Proteins to Amyloids - 1st Edition - ISBN: 9780081029817

From Globular Proteins to Amyloids

1st Edition

Editors: Irena Roterman-Konieczna
Paperback ISBN: 9780081029817
Imprint: Elsevier
Published Date: 2nd October 2019
Page Count: 278
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Description

The phenomenon of amyloidosis has attracted the attention of numerous researchers for two main reasons: (1) it involves unexpected changes in protein conformation (without chemical intervention) and (2) has practical implications, such as elucidating the mechanisms which drive neurodegenerative diseases carries. In particular, understanding the process of amyloidosis is a fundamental prerequisite in the search for new, effective drugs and therapies targeting the key area of neurodegenerative diseases.

The book proposes a model and a mechanism which explain protein misfolding. The concepts presented are based on a model originally intended to show how proteins attain their native conformations.

The model is quantitative in nature and founded upon arguments derived from information theory. It facilitates prediction and simulation of the amyloid fibrillation process. It also identifies progressive changes which occur in native proteins, leading to the emergence of amyloid aggregations.

Key Features

  • The book introduces basic rules for protein folding as well as conditions which result in misfolding
  • The novelty of the presented research lies in treating the aqueous environment as a continuum rather than a set of individual water molecules (i.e. the classic representation)
  • The effect of the environment is modelled as an external force field which affects the folding process at each stage
  • Provides practical applications in helping the prevention of amyloidosis and improving drug design

Readership

Researchers interested in problems related to amyloid formation and protein folding/mis-folding. Students of medicine, pharmacy and pharmacology where protein folding is taught as part of the basic biochemistry curriculum. Pharmaceutical companies which engage in R&D activities related to drug design

Table of Contents

Foreword
Irena Roterman
introduction
Konieczny Leszek and Irena Roterman
1. Description of the fuzzy oil drop model
Banach Mateusz, Konieczny Leszek and Irena Roterman
2. Folding with the active participation of water
Gadzała Małgorzata, Dułak Dawid, Banach Mateusz, Konieczny Leszek, Irena Roterman, Stapor Katarzyna and Fabian Piotr
3. Information coded in protein structure
Konieczny Leszek and Irena Roterman
4. Glubular or ribbon-like micelle
Konieczny Leszek and Irena Roterman
5. Proteins structured as spherical micelles
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. Local discordance
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. A. The active site in a single-chain enzyme identified as local deficiency of hydrophobicity
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. C. Ligand binding cavity coded in form of local defficiency of hydrophobicity
Banach Mateusz, Konieczny Leszek and Irena Roterman
7. Solenoid – amyloid under control
Banach Mateusz and Irena Roterman
8. Composite structures
Banach Mateusz, Irena Roterman and Konieczny Leszek
9. Permanent chaperons
Banach Mateusz and Irena Roterman
9. A. Non-amyloid structure of the aβ(1-42) polypeptide requiring a permanent chaperone
Banach Mateusz and Irena Roterman
9. B. Structural properties of aβ(1-42) chain fragments in complex with proteins acting as permanent chaperones
Banach Mateusz and Irena Roterman
10. Amyloids
Banach Mateusz and Irena Roterman
10. A. Amyloid as a ribbon-like micelle
Banach Mateusz and Irena Roterman
10. B. Alternative conformations of the aβ(1-40) amyloid protein
Gadzała Małgorzata, Dułak Dawid, Banach Mateusz and Irena Roterman
10. C. Specificity of amino acid sequence and its role in secondary and supersecondary structure generation
Banach Mateusz and Irena Roterman
11. Anti-amyloid drug design
Banach Mateusz, Konieczny Leszek and Irena Roterman
12. Predicted structure of the transthyretin amyloid
Banach Mateusz, Konieczny Leszek and Irena Roterman
Summary – the protein is an inteligent micelle
Irena Roterman

Details

No. of pages:
278
Language:
English
Copyright:
© Elsevier 2020
Published:
2nd October 2019
Imprint:
Elsevier
Paperback ISBN:
9780081029817

About the Editor

Irena Roterman-Konieczna

Professor Irena Roterman-Konieczna her 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. She is the Chief Editor of the journal Bio-Algorithms and Med-Systems (de Gruyter).

Affiliations and Expertise

Professor of Bioinformatics, Jagiellonian University, Poland

Ratings and Reviews