Simulating Protein Folding in Variable Environmental Conditions: Transformation from Globular Proteins to Amyloids
Editat de Irena Roterman-Koniecznaen Limba Engleză Paperback – 30 ian 2026
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 α-synuclein, transthyretin endorphin, prefoldin, and chaperonin to demonstrate the role of external force in the protein transformation process
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Specificații
ISBN-13: 9780443404757
ISBN-10: 0443404755
Pagini: 350
Dimensiuni: 152 x 229 mm
Editura: ELSEVIER SCIENCE
ISBN-10: 0443404755
Pagini: 350
Dimensiuni: 152 x 229 mm
Editura: ELSEVIER SCIENCE
Cuprins
Part I: The amyloid transformation
1. The hypothesis - the biochemistry of amyloids
2. Three examples of different scenarios of amyloid transformation
Part II: Role of local environment in proteins structurization
3. Water environment
4. Membrane environment
5. General universal form to express the external force field
Part III: Local environment representation in programs oriented on protein structure prediction
6. Presentation of protocol for In Silico folding simulation Part IV: Specificity of secondary structure in amyloids
7. Analysis of secondary structure specificity as it appears in amyloids
Part V: The complete spectrum of environment influence (external force field) on protein folding
8. The examples of protein representing the micelle-like construction
9. The examples of proteins with participation of external force field in moderate degree
10. The trans-membrane proteins as examples of high influence of local environment on protein structurization
11. Enzymes – their protein body - as objects delivering the local external force field for catalytic reaction
12. Folding in assistance of chaperonin, chaperon, prefoldin – analysis as expressed by FOD-M model
Part VI: Alternative models for amyloid interpretation
13. Alternative models
1. The hypothesis - the biochemistry of amyloids
2. Three examples of different scenarios of amyloid transformation
Part II: Role of local environment in proteins structurization
3. Water environment
4. Membrane environment
5. General universal form to express the external force field
Part III: Local environment representation in programs oriented on protein structure prediction
6. Presentation of protocol for In Silico folding simulation Part IV: Specificity of secondary structure in amyloids
7. Analysis of secondary structure specificity as it appears in amyloids
Part V: The complete spectrum of environment influence (external force field) on protein folding
8. The examples of protein representing the micelle-like construction
9. The examples of proteins with participation of external force field in moderate degree
10. The trans-membrane proteins as examples of high influence of local environment on protein structurization
11. Enzymes – their protein body - as objects delivering the local external force field for catalytic reaction
12. Folding in assistance of chaperonin, chaperon, prefoldin – analysis as expressed by FOD-M model
Part VI: Alternative models for amyloid interpretation
13. Alternative models