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1. |
Record Nr. |
UNINA9910969707703321 |
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Autore |
Steinberg David I. <1928-2024.> |
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Titolo |
The Military in Burma/Myanmar : On the Longevity of Tatmadaw Rule and Influence |
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Pubbl/distr/stampa |
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Singapore : , : ISEAS - Yusof Ishak Institute, , 2021 |
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©2021 |
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Edizione |
[1st ed.] |
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Descrizione fisica |
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1 online resource (1 online resource 45 p.) |
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Disciplina |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based upon print version of record. |
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Sommario/riassunto |
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The Myanmar military has dominated that complex country for most of the period since independence in 1948. The fourth coup of 1 February 2021 was the latest by the military to control those aspects of society it deemed essential to its own interests, and its perception of state interests.The military's institutional power was variously maintained by rule by decree, through political parties it founded and controlled, and through constitutional provisions it wrote that could not be amended without its approval.This fourth coup seems a product of personal demands for power between Senior General. |
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2. |
Record Nr. |
UNINA9910825812403321 |
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Titolo |
Analysis and function of amino acids and peptides / / edited by Andrew B. Hughes |
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Pubbl/distr/stampa |
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Weinheim, Germany, : Wiley-VCH, 2012 |
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ISBN |
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9781299241190 |
1299241190 |
9783527631858 |
3527631852 |
9783527631841 |
3527631844 |
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Edizione |
[1st ed.] |
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Descrizione fisica |
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1 online resource (510 p.) |
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Collana |
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Amino acids, peptides and proteins in organic chemistry ; ; v. 5 |
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Altri autori (Persone) |
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Disciplina |
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Soggetti |
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Amino acids - Analysis |
Peptides - Analysis |
Proteins - Analysis |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based upon print version of record. |
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Nota di bibliografia |
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Includes bibliographical references and index. |
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Nota di contenuto |
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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 Modifications; 1.2.3 Ex Vivo Protein Modifications |
1.3 Sample Preparation and Data Acquisition 1.3.1 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 Identification of Proteins from MS/MS Spectra of Peptides; 1.4.2 De Novo Sequencing; 1.5 MS of Protein Structure, Folding, and |
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Interactions; 1.5.1 Methods to Mass-Tag Structural Features; 1.6 Conclusions and Perspectives; References |
2 X-Ray Structure Determination of Proteins and Peptides 2.1 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 Waves 2.4.2 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 Refining the Structure 2.7.1 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 |
3.2.5 Labile Protons |
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Sommario/riassunto |
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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 |
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