Mass Spectrometry Based Strategies For Biomolecular Structure Analysis
Download Mass Spectrometry Based Strategies For Biomolecular Structure Analysis PDF/ePub or read online books in Mobi eBooks. Click Download or Read Online button to get Mass Spectrometry Based Strategies For Biomolecular Structure Analysis book now. This website allows unlimited access to, at the time of writing, more than 1.5 million titles, including hundreds of thousands of titles in various foreign languages.
Mass Spectrometry-based Strategies for Biomolecular Structure Analysis
Mass spectrometry is an important method for studying the structure of both small molecules and large biomolecules (e.g., proteins). The majority of the applications prior to 1970 were focused on small molecules, owing to the limited ionization methods which posed difficulties in producing gas-phase ions for large biomolecules then. Beginning in the 1980's, with the introduction of new ionization methods (ESI and MALDI), the applications have gradually switched to biological science measuring large bioorganic molecules. Today, with the developing interest in metabolomics and proteomics, and ongoing improvement in MS-based techniques, mass spectrometry is extensively applied in the study of both small and large molecules. The research presented in this thesis falls into two main parts, which focus on the application of MS in (1) structural analysis of steroid metabolites and (2) characterization of protein-protein interactions. In the first part, combinations of different MS methods are adopted and used to solve the structures of unknown steroid metabolites, which are the pheromones responsible for mouse communication in mouse urine. This part includes three chapters, the first two of which discuss the method development of using MS to study the structure of steroid metabolites; and the third chapter presents the application of the MS methods in solving a newly discovered steroid pheromone, which is determined as a sex-specific hormone. In the second part, two MS-based strategies, namely, hydrogen-deuterium exchange (HDX) and fast photochemical oxidation of proteins (FPOP), are applied in two studies of protein-protein interactions, including: (1) dimerization of SecA, which is a motor protein in bacteria translocation pathway; and (2) interface mapping of EGFR binding to Adnectin1. In the first chapter in Part 2, we used HDX MS to characterize the dimer interface of SecA, and, meanwhile, detected a conformational change from open to closed forms at the pre-protein binding domain upon dimerization. This conformational change provided leads for the active form of SecA. In the second chapter in Part 2, we applied FPOP, which is modified to suit therapeutic protein formulation conditions, to map the epitope of Adnectin1-EGFR interaction at amino acid residue level. The epitope identified agrees with that from both HDX study and crystallography results, presenting more evidence of the capability of FPOP in epitope mapping. These five studies on characterization of steroid metabolites and protein-protein interactions show the successful application of mass spectrometry in the structural study of both small molecules and large proteins. Furthermore, there's a great potential for study of more complex systems.
Advanced Spectroscopic Methods to Study Biomolecular Structure and Dynamics
Advanced Spectroscopic Methods to Study Biomolecular Structure and Dynamics presents the latest emerging technologies in spectroscopy and advances in established spectroscopic methods. The book presents a guide to research methods in biomolecular spectroscopy, providing comprehensive coverage of developments in the spectroscopic techniques used to study protein structure and dynamics. Seventeen chapters from leading researchers cover key aspects of spectroscopic methods, with each chapter covering structure, folding, and dynamics. This title will help researchers keep up-to-date on the latest novel methods and advances in established methods. - Presents current, emerging, and evolving advances and applications of spectroscopic techniques in the study of biomolecules, including proteins and nucleic acids - Discusses contemporary spectroscopic techniques used to study biomolecular structure, interaction, and dynamics
New Methods for the Study of Biomolecular Complexes
Author: W. Ens
language: en
Publisher: Springer Science & Business Media
Release Date: 2013-03-09
A NATO Advanced Research Workshop entitled New Methods for the Study of Molecular Aggregates was held at Tbe Lodge at Kananaskis Village, Alberta, Canada from 16 -20 June 1996. In fact the meeting was entirely concerned with the problem of analyzing biomolecular complexes, so the title of these proceedings has been altered to give a more precise description of the content. Tbe workshop was hosted by the time-of-flight group of the Department of Physics at the University of Manitoba, and was attended by 64 participants from around the world. '!\venty-one invited talks were given and 27 papers were presented as posters. Of the 48 contributions, 22 papers (12 orals, 10 posters) are included in these proceedings. Tbe subject of the conference was the investigation of noncovalent biomolecular complexes, with particular focus on the application of mass spectrometry to their characterization. '!\vo new ionization techniques introduced in the late 1980s, electrospray ionization (ES I) and matrix-assisted laser desorptionlionization (MALDI), resulted in a breakthrough in mass spectrometry, enabling its use in molecular weight and primary structure determination of biopolymers larger than 100 kDa. Recently it has been discovered that ESI mass spectrometry mayaiso be used to characterize complexes containing noncovalent interactions, thus opening new perspectives for supramolecular chemistry. ESI mass spectrometry has the advantage that the sampie is introduced from a homogenous solution which can be maintained at near physiological conditions of pR, concentration, and temperature.