Encyclopedia of Spectroscopy and Spectrometry


Book Description

This third edition of the Encyclopedia of Spectroscopy and Spectrometry, Three Volume Set provides authoritative and comprehensive coverage of all aspects of spectroscopy and closely related subjects that use the same fundamental principles, including mass spectrometry, imaging techniques and applications. It includes the history, theoretical background, details of instrumentation and technology, and current applications of the key areas of spectroscopy. The new edition will include over 80 new articles across the field. These will complement those from the previous edition, which have been brought up-to-date to reflect the latest trends in the field. Coverage in the third edition includes: Atomic spectroscopy Electronic spectroscopy Fundamentals in spectroscopy High-Energy spectroscopy Magnetic resonance Mass spectrometry Spatially-resolved spectroscopic analysis Vibrational, rotational and Raman spectroscopies The new edition is aimed at professional scientists seeking to familiarize themselves with particular topics quickly and easily. This major reference work continues to be clear and accessible and focus on the fundamental principles, techniques and applications of spectroscopy and spectrometry. Incorporates more than 150 color figures, 5,000 references, and 300 articles for a thorough examination of the field Highlights new research and promotes innovation in applied areas ranging from food science and forensics to biomedicine and health Presents a one-stop resource for quick access to answers and an in-depth examination of topics in the spectroscopy and spectrometry arenas







Final Report. Surface-induced Dissociation Versus Collision-induced Dissociation


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A 7-Tesla Fourier transform ion-cyclotron resonance (FTICR) mass spectrometer was modified to insert a surface inside the cell for ion-surface collisions leading to the dissociation of impacting ions. Modifications were made to the software/hardware to collide the ions brought into the cell and trap the resulting fragment and undissociated primary ions inside the cell. The trapping plates were also ramped to determine kinetic energy distributions of these ions. The surface-induced dissociation (SID) of benzene and chromium hexacarbonyl ions was first studied as test cases for the instrument. Then a systematic study of the SID of small protonated peptides formed by electrospray ionization was begun. A series of small alanine(A)-containing peptides, viz., AA, AAA, AAAA, AAAAA, and PAAAA were used in the study. In the absence of any direct comparisons of the SID processes with the commonly used technique of tandem mass spectrometry of collision-induced dissociations (CID) via collisions with a neutral gas, a comparative study of CID and SID using the same protonated peptides was made. Since multiple collisions are often used to enhance dissociation efficiency in CID, the CID was performed under single as well as multiple collisional activation conditions. Both on-resonance and sustained off-resonance irradiation excitation were used for CID experiments. Kinetic energy of the ions was varied by changing peak-to-peak voltage applied to the excitation plates. Results are shown in a series of graphs, and a simple theoretical model is presented. This direct comparison of the two activation techniques on the same instrument provided insights into the similarities and differences between these two. The results suggest that internal energy distributions of ions activated by ion-surface collision and multiple collision ion-gaseous neutral collisions are quite comparable. The results also suggest that, in ion-surface collisions, the ion collides with only a small fraction of th e self-assembled monolayer chain, making it effectively a process very similar to CID.







DDR Bezirk Dresden


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Collision Velocity Dependence of Products Formed Via Surface Induced Dissociation


Book Description

Analysis of large molecules from proteins to peptides and even higher mass species such as DNA is an important task, and in recent years, has been a specialty of mass spectrometry. Gaining structural information is possible using multi stage mass spectrometric techniques (MS) n . The technique of surface induced dissociation (SID) of singly protonated peptides ionized by matrix assisted laser desorption/ionization and analyzed by a tandem time-of-flight mass spectrometer with a collision surface located between the two time-of-flight mass spectrometers is described here. The identity of positively charged product ions from SID is dependent on the velocity of the parent ions colliding at near normal angles to the SID surface. This dependence on collision velocity is evident for the entire mass range of peptides studied (280-12,384 amu). The observed trend suggests that SID has the potential to fragment very large ions, yielding product ions of certain identities, as long as, the necessary collision energy/velocity can be achieved. SID of the protonated peptides produces product ions that fall into categories of the following types of product ions: intact molecular ions, backbone fragments, single amino acid immonium ions (H 2 N = CH-R) +, immonium ion fragments, and finally, sputtered surface material. The range of collision energies over which these products occurs changes based upon the mass of the ion, but is constant for collision velocity. The ranges of collision velocities for the different types of product ions are as follows: intact molecular ions and backbone fragments (3500 m/s), single amino acid immonium ions (2600-5000 m/s), fragments of immonium ions (5000-13,000 m/s), and sputtered ions from the surface (13,200 m/s).







Spectroscopy and Modeling of Biomolecular Building Blocks


Book Description

Spectroscopy and Modeling of Biomolecular Building Blocks presents an overview of recent advances in the intertwining of the following research fields: photon and electron spectroscopy, quantum chemistry, modelling and mass-spectrometry. The coupling of these disciplines offers a new point of view to the understanding of isolated elementary building blocks of biomolecules and their assemblies. It allows the unambiguous separation between intrinsic properties of biomolecular systems and those induced by the presence of their environment. The first chapters provide background in modelling (I), frequency-resolved spectroscopy using microwave, infrared and UV photons, time-resolved spectroscopy in the femtosecond domain and energy-resolved electron spectroscopy (II) and production of gas-phase neutral and ionic biomolecular species, mass-spectrometry, ion mobility and BIRD techniques (III). Chapter IV is devoted to case studies of gas-phase experimental investigations coupled to quantum or classical calculations. The topics are structural studies of nucleobases and oligonucleotides, peptides and proteins, sugars; neuromolecules; non-covalent complexes; chiral systems, interactions of low-energy electrons with biomolecules in the radiation chemistry context and very large gas-phase biomolecular systems. The fifth chapter concerns the link between gas-phase and liquid-phase. Different treatments of solvation are illustrated through examples pointing out the influence of progressive addition of water molecules upon properties of nucleobases, peptides, sugars and neuromolecules. Offer a new perspective to the understanding of isolated elementary building blocks of bio molecules Includes case studies of experimental investigations coupled to quantum or classical calculations