Simulating Protein Folding in Variable Environmental Conditions

Nyhet

Transformation from Globular Proteins to Amyloids

Häftad, Engelska, 2026

1 839 kr

Kommande

Simulating Protein Folding in Variable Environmental Conditions: Transformation from Globular Proteins to Amyloids delves into the effects of external conditions upon the protein folding process. The book considers how this can lead to amyloid formation and why proteins fold the way they do. It presents the fuzzy oil drop model (FOD-M), which enables the measurements of external factors influencing the folding process and considers changed external conditions as the source for the misfolding process. Sections provide an introduction to amyloid transformation and outline the hypothesis of the model simulation before considering the role of environmental factors, including the water environment and membrane environment.

This book is a useful resource for researchers interested in investigating protein folding across molecular biology, structural biology, biochemistry, computational biology and related fields.

Offers a model for simulating amyloid transformation in silico
Explores how external properties influence the structural rearrangement of proteins
Considers various types of amyloids, including ?-synuclein, transthyretin endorphin, prefoldin, and chaperonin to demonstrate the role of external force in the protein transformation process

Produktinformation

Utgivningsdatum2026-01-30
Mått152 x 229 x undefined mm
Vikt450 g
FormatHäftad
SpråkEngelska
Antal sidor350
FörlagElsevier Science
ISBN9780443404757

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Biologi inom Naturvetenskap och teknik

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).

Part I: The amyloid transformation1. The hypothesis - the biochemistry of amyloids2. Three examples of different scenarios of amyloid transformationPart II: Role of local environment in proteins structurization3. Water environment4. Membrane environment5. General universal form to express the external force fieldPart III: Local environment representation in programs oriented on protein structure prediction6. Presentation of protocol for In Silico folding simulation Part IV: Specificity of secondary structure in amyloids7. Analysis of secondary structure specificity as it appears in amyloidsPart V: The complete spectrum of environment influence (external force field) on protein folding8. The examples of protein representing the micelle-like construction9. The examples of proteins with participation of external force field in moderate degree10. The trans-membrane proteins as examples of high influence of local environment on protein structurization11. Enzymes – their protein body - as objects delivering the local external force field for catalytic reaction12. Folding in assistance of chaperonin, chaperon, prefoldin – analysis as expressed by FOD-M modelPart VI: Alternative models for amyloid interpretation13. Alternative models