Textbook Of Structural Biology (Second Edition)World Scientific, 2016 M09 27 - 612 páginas This book provides a comprehensive coverage of the basic principles of structural biology, as well as an up-to-date summary of some main directions of research in the field. The relationship between structure and function is described in detail for soluble proteins, membrane proteins, membranes, and nucleic acids.There are several books covering protein structure and function, but none that give a complete picture, including nucleic acids, lipids, membranes and carbohydrates, all being of central importance in structural biology.The book covers state-of-the-art research in various areas. It is unique for its breadth of coverage by experts in the fields. The book is richly illustrated with more than 400 color figures to highlight the wide range of structures. |
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Página 11
... atoms forms if the resulting arrangement of the two nuclei and their electrons has a lower energy than the total energy of the separate atoms. If the lowest energy is obtained by a complete transfer of one or more electrons from one atom ...
... atoms forms if the resulting arrangement of the two nuclei and their electrons has a lower energy than the total energy of the separate atoms. If the lowest energy is obtained by a complete transfer of one or more electrons from one atom ...
Página 12
... atoms link through a covalent bond and discrete molecules are formed, such as H2 and NH3 . For biological macromolecules the covalent bond is the most frequently occurring one. Hydrogen bonds are also very prevalent (see Section 2.1.4) ...
... atoms link through a covalent bond and discrete molecules are formed, such as H2 and NH3 . For biological macromolecules the covalent bond is the most frequently occurring one. Hydrogen bonds are also very prevalent (see Section 2.1.4) ...
Página 13
... atoms become protonated. The red-ox properties of such interactions are of great impor- tance to certain proteins. The distance between the sulfur atoms in a disulfide bond is around 2 Å. 2.1.3. Charge. Interactions. Electrostatic ...
... atoms become protonated. The red-ox properties of such interactions are of great impor- tance to certain proteins. The distance between the sulfur atoms in a disulfide bond is around 2 Å. 2.1.3. Charge. Interactions. Electrostatic ...
Página 14
... atoms with lone electron pairs (called the donor and acceptor) can form a hydrogen bond. These terms indicate that ... atoms, where the donor has a covalently bound hydrogen and the acceptor has a free electron pair. Hydrogen bonds ...
... atoms with lone electron pairs (called the donor and acceptor) can form a hydrogen bond. These terms indicate that ... atoms, where the donor has a covalently bound hydrogen and the acceptor has a free electron pair. Hydrogen bonds ...
Página 15
... atom ( Figure 2.1 ) . Because all four a - carbon substituents are different , amino acids pos- sess an inherent chirality . This means that their mirror images are unique molecules that are not superimposable on each other ( Figure 2.1 ) ...
... atom ( Figure 2.1 ) . Because all four a - carbon substituents are different , amino acids pos- sess an inherent chirality . This means that their mirror images are unique molecules that are not superimposable on each other ( Figure 2.1 ) ...
Contenido
1 | |
11 | |
37 | |
Chapter 4 Basics of Membrane Proteins | 69 |
Chapter 5 Basics of Nucleic Acid Structure | 105 |
Chapter 6 Basics of Lipids and Membrane Structure | 161 |
Chapter 7 Basics of Carbohydrates | 213 |
Chapter 8 Enzymes | 227 |
Chapter 12 Protein Folding and Degradation | 385 |
Chapter 13 Transmembrane Transport | 425 |
Chapter 14 Signal Transduction | 451 |
Chapter 15 Cell Motility and Transport | 481 |
Chapter 16 Structural Aspects of CellCell Interactions | 507 |
Chapter 17 The Immune System | 521 |
Chapter 18 Virus Structure and Function | 535 |
Chapter 19 Bioinformatics Tools in Structural Biology | 553 |
Chapter 9 Genome Structure DNA Replication and Recombination | 269 |
Chapter 10 Transcription | 307 |
Chapter 11 Protein Synthesis Translation | 351 |
Index | 577 |
Otras ediciones - Ver todas
Textbook Of Structural Biology Anders Liljas,Lars Liljas,Jure Piskur,Goran Lindblom,Poul Nissen,Morten Kjeldgaard Vista previa limitada - 2009 |
Términos y frases comunes
AAA+ acid residues actin actin fiber active amino acid antiparallel arginine atoms ATPase backbone bacteria base pairs binding bound catalytic cell cellular chaperones complex conformational changes core crystal structure dimer DNA polymerase domain EF-Tu enzyme eukaryotic example extracellular factor Figure filaments fold function fusion G-proteins gene groove helicase helices helix histone hydrogen bonds hydrolysis hydrophobic integrin interactions interface involved kinase ligand linker lipid bilayer loop mechanism membrane proteins modules molecular monomers motif mRNA myosin N-terminal nucleosomes nucleotide pathway peptide phase phosphate polar polypeptide protease proteasome proton RecA receptor region replication ribose ribosome Right role rRNA secondary structure Section sequence shown side chains signal similar specific ẞ subunits stability strand substrate surface switch symmetry synthase synthesis teins template tion topology transcription transmembrane transmembrane helices transport trimeric tRNA tyrosine virus viruses water molecule