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Amino Acids, Peptides and Proteins in Organic Chemistry, Analysis and Function of Amino Acids and Peptides : Analysis and Function of Amino Acids and Peptides.
This is the last of five books in the Amino Acids, Peptides and Proteins in Organic Synthesis series. Closing a gap in the literature, this is the only series to cover this important topic in organic and biochemistry. Drawing upon the combined expertise of the international ""who's wh...
| Clasificación: | Libro Electrónico |
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| Autor principal: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Weinheim :
Wiley,
2013.
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| Colección: | Amino Acids, Peptides and Proteins in Organic Chemistry (VCH)
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| Temas: | |
| Acceso en línea: | Texto completo |
Tabla de Contenidos:
- Amino Acids, Peptides and Proteins in Organic Chemistry:Volume 5
- Analysis and Function of Amino Acids and Peptides; Contents; List of Contributors; 1 Mass Spectrometry of Amino Acids and Proteins; 1.1 Introduction; 1.1.1 Mass Terminology; 1.1.2 Components of a Mass Spectrometer; 1.1.3 Resolution and Mass Accuracy; 1.1.4 Accurate Analysis of ESI Multiply Charged Ions; 1.1.5 Fragment Ions; 1.2 Basic Protein Chemistry and How it Relates to MS; 1.2.1 Mass Properties of the Polypeptide Chain; 1.2.2 In Vivo Protein Modi.cations; 1.2.3 Ex Vivo Protein Modi.cations.
- 1.3 Sample Preparation and Data Acquisition1.3.1 Top-Down Versus Bottom-Up Proteomics; 1.3.2 Shotgun Versus Targeted Proteomics; 1.3.3 Enzymatic Digestion for Bottom-Up Proteomics; 1.3.4 Liquid Chromatography and Capillary Electrophoresis for Mixtures in Bottom-Up; 1.4 Data Analysis of LC-MS/MS (or CE-MS/MS) of Mixtures; 1.4.1 Identi.cation of Proteins from MS/MS Spectra of Peptides; 1.4.2 De Novo Sequencing; 1.5 MS of Protein Structure, Folding, and Interactions; 1.5.1 Methods to Mass-Tag Structural Features; 1.6 Conclusions and Perspectives; References.
- 2 X-Ray Structure Determination of Proteins and Peptides2.1 Introduction; 2.1.1 Light Microscopy; 2.1.2 X-Rays and Crystallography at the Start; 2.1.3 X-Ray Crystallography Today; 2.1.4 Limitations of X-Ray Crystallography; 2.2 Growing Crystals; 2.2.1 Why Crystals?; 2.2.2 Basic Methods of Growing Protein Crystals; 2.2.3 Protein Sample; 2.2.4 Preliminary Crystal Analysis; 2.2.5 Mounting Crystals for X-Ray Analysis; 2.3 Symmetry and Space Groups; 2.3.1 Crystals and the Unit Cell; 2.3.2 Point Groups; 2.3.3 Space Groups; 2.3.4 Asymmetric Unit; 2.4 X-Ray Scattering and Diffraction.
- 2.4.1 X-Rays and Mathematical Representation of Waves2.4.2 Interaction of X-Rays with Matter; 2.4.3 Crystal Lattice, Miller Indices, and the Reciprocal Space; 2.4.4 X-Ray Diffraction from a Crystal: Bragg.s Law; 2.4.5 Bragg.s Law in Reciprocal Space; 2.4.6 Fourier Transform Equation from a Lattice; 2.4.7 Friedel' s Law and the Electron Density Equation; 2.5 Collecting and Processing Diffraction Data; 2.5.1 Data Collection Strategy; 2.5.2 Symmetry and Scaling Data; 2.6 Solving the Structure (Determining Phases); 2.6.1 Molecular Replacement; 2.6.2 Isomorphous Replacement; 2.6.3 MAD.
- 2.7 Analyzing and Re.ning the Structure2.7.1 Electron Density Interpretation and Model Building; 2.7.2 Protein Structure Refinement; 2.7.3 Protein Structure Validation; References; 3 Nuclear Magnetic Resonance of Amino Acids, Peptides, and Proteins; 3.1 Introduction; 3.1.1 Active Nuclei in NMR; 3.1.2 Energy Levels and Spin States; 3.1.3 Main NMR Parameters (Glossary); 3.1.3.1 Chemical Shift; 3.1.3.2 Scalar Coupling Constants; 3.1.3.3 NOE; 3.1.3.4 RDC; 3.2 Amino Acids; 3.2.1 Historical Significance; 3.2.2 Amino Acids Structure; 3.2.3 Random Coil Chemical Shift; 3.2.4 Spin Systems.