Thesis (Ph. D.)--University of Wisconsin, 1967. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

Call number: LD2668 .T4 1951 M373 / Master of Science

No description available.

No description available.

The anistropy of the orbital and spin properties of conduction electrons in InSb has been measured simultaneously using a cyclotron-resonance type experiment. This represents the first time that the anistropy of effective mass in InSb has been directly measured using an optical method.

Call number: LD2668 .T4 1950 J69 / Master of Science

by Ng King-man. / Bibliography: leaves 87-89 / Thesis (M.Ph.)--Chinese University of Hong Kong, 1986

Digitized by Kansas Correctional Industries

Digitized by Kansas Correctional Industries

Wong, Pui Shuen. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2011. / Includes bibliographical references (leaves 92-96). / Abstracts in English and Chinese. / Title Page --- p.i / Abstract (English) --- p.ii / Abstract (Chinese) --- p.iii / Acknowledgements --- p.iv / Table of Contents --- p.V / List of Tables --- p.viii / List of Figures --- p.ix / List of Schemes --- p.xi / Symbols and Abbreviations --- p.xii / Dedication --- p.xiv / Chapter Chapter 1 --- Introduction / Chapter 1.1 --- Mass Spectrometry of peptides/ proteins --- p.1 / Chapter 1.1.1 --- Electrospray ionization of peptides/ proteins --- p.3 / Chapter 1.2 --- Tandem mass spectrometry of peptides/ proteins --- p.4 / Chapter 1.2.1 --- Nomenclature of peptide fragment ions --- p.5 / Chapter 1.2.2 --- Slow heating methods for MSn --- p.6 / Chapter 1.2.2.1 --- Collision induced dissociation --- p.7 / Chapter 1.2.3 --- "Electron based ion activation for MS""" --- p.8 / Chapter 1.3 --- Electron Capture Dissociation --- p.9 / Chapter 1.3.1 --- ECD mechanism for protonated peptide ions --- p.10 / Chapter 1.3.2 --- ECD efficiency --- p.12 / Chapter 1.3.3 --- ECD of metal ions-adducted peptide --- p.13 / Chapter 1.4 --- Overview of present work --- p.14 / Chapter Chapter 2 --- "Instrumentation, Experimental and Calculations" / Chapter 2.1 --- Fourier-transform Ion Cyclotron Resonance Mass Spectrometer --- p.15 / Chapter 2.1.1 --- Basic principle of FTICR-MS --- p.15 / Chapter 2.1.2 --- The instrument --- p.19 / Chapter 2.1.2.1 --- Vacuum system --- p.19 / Chapter 2.1.2.2 --- Nanospray source --- p.24 / Chapter 2.1.2.3 --- Electrostatic ion focusing system --- p.26 / Chapter 2.1.2.4 --- Infinity´ёØ Cell --- p.28 / Chapter 2.1.2.5 --- Electron emission source --- p.29 / Chapter 2.1.2.6 --- Data acquisition system --- p.31 / Chapter 2.2 --- Experimental --- p.31 / Chapter 2.2.1 --- Acquisition pulse program --- p.31 / Chapter 2.2.1.1 --- Simple ESI acquisition pulse program (MS experiment) --- p.31 / Chapter 2.2.1.2 --- ESI-ECD acquisition pulse program (MS experiment) --- p.34 / Chapter 2.2.2 --- Molecular mechanics calculation --- p.36 / Chapter Chapter 3 --- Structural Parameters Affecting Suppression of N-Ca Cleavages of Peptides Ions after Electron Capture / Chapter 3.1 --- Introduction --- p.37 / Chapter 3.2 --- Experimental section --- p.39 / Chapter 3.3 --- Results and Discussion --- p.40 / Chapter 3.3.1 --- Peptides with three arginine residues --- p.40 / Chapter 3.3.1.1 --- General ECD mass spectra features --- p.40 / Chapter 3.3.1.2 --- Comparison of the extent of suppression of triariginated and diarginated model peptides ions --- p.46 / Chapter 3.3.2 --- Peptides with histidine and lysine as proton carriers --- p.47 / Chapter 3.3.2.1 --- General features of ECD mass spectra --- p.47 / Chapter 3.3.2.2 --- Comparison of ECD behavior of peptide ions with different proton carrier --- p.50 / Chapter 3.3.3 --- Peptides with various chain length --- p.53 / Chapter 3.3.3.1 --- General ECD mass spectra features --- p.53 / Chapter 3.3.3.2 --- Reactivation of [M+2H]+* by collision activation --- p.57 / Chapter 3.3.3.3 --- Significance of glutamic acid residues --- p.57 / Chapter 3.3.3.4 --- Results of conformational searches --- p.60 / Chapter 3.4 --- Conclusions --- p.64 / Chapter Chapter 4 --- Investigation of the Role of Conformation of Peptide Ions in Suppression of Backbone fragmentation / Chapter 4.1 --- Introduction --- p.67 / Chapter 4.2 --- Experimental section --- p.69 / Chapter 4.3 --- Results and Discussion --- p.70 / Chapter 4.3.1 --- Peptide with N-methylated amino acid residues --- p.70 / Chapter 4.3.1.1 --- General features of ECD mass spectra --- p.70 / Chapter 4.3.1.2 --- Comparison between normal and N-methylated peptide ions under ECD --- p.72 / Chapter 4.3.2 --- Peptides with proline residues vi --- p.73 / Chapter 4.3.2.1 --- General ECD mass spectra features --- p.73 / Chapter 4.3.2.2 --- Comparison of ECD of peptide ions with and without proline residues --- p.76 / Chapter 4.3.3 --- Transition metal ions as charge carriers --- p.80 / Chapter 4.3.3.1 --- General ECD mass spectra features --- p.80 / Chapter 4.3.3.2 --- Comparison of ECD behavior using proton and metal ions as charge carrier --- p.85 / Chapter 4.4 --- Conclusions --- p.87 / Chapter Chapter 5 --- Conclusions --- p.90 / References --- p.92 / Chapter Appendix I --- Twenty common amino acids --- p.97 / Chapter Appendix II --- Pulse programs for MS and MSn experiments --- p.98