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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 Andrew B Hughes

  • SKU: BELL-4335212
Amino Acids Peptides And Proteins In Organic Chemistry Analysis And Function Of Amino Acids And Peptides Analysis And Function Of Amino Acids And Peptides Andrew B Hughes
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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 Andrew B Hughes instant download after payment.

Publisher: Royal Society of Chemistry
File Extension: PDF
File size: 9.11 MB
Pages: 510
Author: Andrew B Hughes
ISBN: 9783527631858, 3527631852
Language: English
Year: 2013

Product desciption

Amino Acids Peptides And Proteins In Organic Chemistry Analysis And Function Of Amino Acids And Peptides Analysis And Function Of Amino Acids And Peptides Andrew B Hughes by Andrew B Hughes 9783527631858, 3527631852 instant download after payment.

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 who"" in amino acid research, these volumes represent a real benchmark for amino acid chemistry, providing a comprehensive discussion of the occurrence, uses and applications of amino acids and, by extension, their polymeric forms, peptides and proteins. The practical value of each volume is h. Read more... Content: 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. Abstract: 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 who"" in amino acid research, these volumes represent a real benchmark for amino acid chemistry, providing a comprehensive discussion of the occurrence, uses and applications of amino acids and, by extension, their polymeric forms, peptides and proteins. The practical value of each volume is h

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