Natalya Kurochkina
Protein Structure and Modeling
Natalya Kurochkina
Protein Structure and Modeling
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This book will consider principles of the organization of protein molecules, the relationships between primary, secondary, and tertiary structure, the determinants of protein conformation, and the applications of structure determination and structure modeling in biomedical research.
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This book will consider principles of the organization of protein molecules, the relationships between primary, secondary, and tertiary structure, the determinants of protein conformation, and the applications of structure determination and structure modeling in biomedical research.
Produktdetails
- Produktdetails
- Verlag: Springer / Springer Nature Singapore / Springer, Berlin
- Artikelnr. des Verlages: 978-981-13-6600-0
- 1st ed. 2019
- Seitenzahl: 284
- Erscheinungstermin: 18. Juni 2019
- Englisch
- Abmessung: 241mm x 160mm x 20mm
- Gewicht: 608g
- ISBN-13: 9789811366000
- ISBN-10: 9811366004
- Artikelnr.: 54952060
- Verlag: Springer / Springer Nature Singapore / Springer, Berlin
- Artikelnr. des Verlages: 978-981-13-6600-0
- 1st ed. 2019
- Seitenzahl: 284
- Erscheinungstermin: 18. Juni 2019
- Englisch
- Abmessung: 241mm x 160mm x 20mm
- Gewicht: 608g
- ISBN-13: 9789811366000
- ISBN-10: 9811366004
- Artikelnr.: 54952060
CHAPTER 1 - Protein Structure
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 - Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 - Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 - Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 - Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 - Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 - Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary
CHAPTER 1 - Protein Structure
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 – Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 – Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 – Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 – Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 – Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 – Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary
CHAPTER 1 - Protein Structure
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 - Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 - Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 - Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 - Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 - Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 - Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary
CHAPTER 1 - Protein Structure
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 – Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 – Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 – Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary
1.1 Polypeptide chain
1.2 Ligand binding
1.3 Active site
1.3 Structure-function
CHAPTER 2 - Conformational transitions
2.1 Types of transitions in molecular systems
2.2 Conformational states
2.3 Quantum motions
2.4 Myoglobin and hemoglobin
2.5 Cytochromes
2.6 Tobacco mosaic virus coat protein
2.7 Fibrin-fibrinogen
2.8 Conformational changes of side chains in protein interior as a basis of the conformational states of the molecule
CHAPTER 3 – Allosteric regulation
3.1 Proteins
3.2 Nucleic acids
3.3 Small ligands
CHAPTER 4 – Protein channels
4.1 Structure-function
4.2 Signaling
CHAPTER 5 - Helical assemblies
5.1 Determinants of specific helix recognition
5.2 Types of assemblies
CHAPTER 6 - multiprotein complexes
6.1 Postsynaptic density
6.2 Viruses
6.3 Implications in signaling
CHAPTER 7 - Methods of structure determination
7.1 X-Ray crystallography, NMR and Electron Microscopy
7.2 NMR
7.3 Electron Microscopy
CHAPTER 8 – Protein modeling
8.1 Helix and its interactions
8.2 Ligands
8.3 Dynamics
References
Dictionary