Buch, Englisch, 240 Seiten, Gewicht: 500 g
Protein folding versus protein structure prediction
Buch, Englisch, 240 Seiten, Gewicht: 500 g
ISBN: 978-1-907568-17-6
Verlag: Woodhead Publishing
Autoren/Hrsg.
Fachgebiete
- Technische Wissenschaften Verfahrenstechnik | Chemieingenieurwesen | Biotechnologie Biotechnologie Medizinische Biotechnologie
- Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Vorklinische Medizin: Grundlagenfächer Molekulare Medizin, Zellbiologie
- Naturwissenschaften Biowissenschaften Proteinforschung
Weitere Infos & Material
Dedication
List of figures
List of tables
About the editor
List of contributors
Introduction
Chapter 1: The early-stage intermediate
Abstract
1.1 Geometric model
1.2 Structural alphabet
1.3 Contingency table
1.4 In search of structural similarities
Chapter 2: The late-stage intermediate
Abstract:
2.1 The " fuzzy oil drop � model
2.2 Quantitative description of the hydrophobic core
2.3 Protein characteristics with respect to the hydrophobic core
2.4 Simulation of late-stage folding
Chapter 3: Structural information involved in the interpretation of the stepwise protein folding process
Abstract:
3.1 Balancing the quantity of information in the amino acid sequence and the early-stage intermediate
3.2 Zones on the Ramachandran map
Chapter 4: The divergence entropy characterizing the internal force field in proteins
Abstract:
4.1 Internal force field for nonbonding interactions
4.2 The impact of ligands
4.3 Structures of homodimers - protein-protein interaction
4.4 Protein containing a catalytic center
4.5 The role of exons
4.6 Conclusions
Chapter 5: Ligand-binding-site recognition
Abstract:
5.1 General model
5.2 ROC curves
5.3 Summary
Chapter 6: Use of the �?ofuzzy oil drop�?� model to identify the complexation area in protein homodimers
Abstract:
6.1 General description
6.2 ROC curves
6.3 Conclusions
Chapter 7: Simulation of the polypeptide chain folding process using the "fuzzy oil drop" model
Abstract:
7.1 Simulation of the folding process in the presence of an external hydrophobic force field
7.2 Folding in the presence of a ligand
7.3 Influence of external factors on polypeptide chain folding
Chapter 8: Misfolded proteins
Abstract:
8.1 Introduction
8.2 In silico experiment
8.3 Conclusions
8.4 Appendix�1: details of the molecular dynamics simulation
8.5 Appendix�2: details of the cluster analysis
Chapter 9: A Short description of other selected ab initio methods for protein structure prediction
Abstract:
9.1 Introduction
9.2 Simplifying the geometric model and the field function
9.3 Lattice model
9.4 ROSETTA
9.5 In search of a global minimum - force field deformation
Chapter 10: Conclusion
Abstract:
10.1 Acknowledgements
Index