Spectroscopic biological application

Second is the application of a wide range of experimental designs and techniques. DNA CT is observed in a diverse array of systems over different distance and time regimes. Consequently, a versatile approach which draws upon complementary methods is required to explore different facets of this chemistry and develop a complete picture. We interrogate a variety of nucleic acid assemblies using spectroscopic, biochemical and electrochemical tools to define mechanistic features, exploit biological applications, and explore biological consequences of DNA CT. 

Spectroscopic Methods, [Biological] Applications of Spectroscopy, EPR, Recent Advances in (Smaller). Spectroscopy, Infrared, Use in Biology (Lecomte). Spectroscopy of Transition-Group Complexes (Jorgensen) Statistical-Mechanical Theory of Transport Processes. X. The Heat of Transport in Binary Liquid Systems (Bearman, Kirkwood, Fixman). ... 

Phosphorus has become an important platform furnace element. It is not as sensitive as most other elements because the resonance lines are not spectroscopically available. But reliable determinations at the ng level can be made in biological materials. It is particularly important to use the platform, matrix modifier and A signals. Consult Curtius et al. (1987) for a thorough discussion of biological applications of the STPF method for P. 

The study of fluorescence of molecules situated near nano-sized metal particles has been the subject of considerable experimental interest in recent years, largely due to important biological applications and the emergence of nano-technology. The spectroscopic properties of molecules interacting with small solid-state particles was investigated theoretically and experimentally over two decades ago. The work pointed to a competition between enhanced radiative processes and additional non-radiative chaimels introduced by the presence of particles. It was found that the specific optical properties of the solid played an important role, as well as the geometric shape of the particle, and the location of the molecule relative to the particle. 

Coherent anti-Stokes Raman (CARS) scattering spectroscopy probes vibrational levels based on a coherent non-linear wave mixing process and is a powerful technique for the vibrational imaging of biological structures. Daniel L. Marks and Stephen A. Boppart discuss new pulse-shaping and interferometry schemes in CARS that improve its spectroscopic capability for biological applications. 

Information concerning the coordination geometry and dynamics of metal-binding sites in proteins can be obtained from perturbed angular correlation of y-rays (PAC) spectroscopy. The underlying theory of this nuclear spectroscopic method is described in detail in [78] and with special emphasis on biological applications in [79,80]. PAC provides means to determine the nuclear quadrupole interaction at the site of an appropriate nucleus used as a spectroscopic probe. The nuclear quadrupole interactiOTi (NQI) describes the interaction between the electric quadrupole moment... 

The opening sentence above says it all. NMR is by far the most valuable spectroscopic technique for structure determination. Although wei) just give an overview of the subject in this chapter, focusing on NMR applications to small molecules, more advanced NMR techniques are also used in biological chemistry to study protein structure and folding. 

The use of Upid bilayers as a relevant model of biological membranes has provided important information on the structure and function of cell membranes. To utilize the function of cell membrane components for practical applications, a stabilization of Upid bilayers is imperative, because free-standing bilayer lipid membranes (BLMs) typically survive for minutes to hours and are very sensitive to vibration and mechanical shocks [156,157]. The following concept introduces S-layer proteins as supporting structures for BLMs (Fig. 15c) with largely retained physical features (e.g., thickness of the bilayer, fluidity). Electrophysical and spectroscopical studies have been performed to assess the appUcation potential of S-layer-supported lipid membranes. The S-layer protein used in aU studies on planar BLMs was isolated fromB. coagulans E38/vl. 

The interaction of dihalogens, particularly diiodine, with sulfur and selenium electron donors has been an area of increasing interest over the past decade because of potential biological, pharmaceutical, and electronic materials applications [35,179]. Devillanova and coworkers have recently reviewed the solution behavior of a large number of chalcogenides and I2, particularly thiones, selones, sulfides, and selenides [180]. Correlations between computational methods, thermodynamic parameters, and spectroscopic data (UV/Vis, 13C NMR, Raman, UPS) were discussed. 

The study of metals in biological systems requires techniques, some of them highly specific, some limited to certain aspects of the metal ion in question, some of more general applicability. Thus, Mossbauer spectroscopy in biological systems is restricted to iron-containing systems because the only element available with a Mossbauer nucleus is 57Fe. The EPR spectroscopic techniques will be of application only if the metal centre has an unpaired electron. In contrast, provided that crystals can be obtained, X-ray diffraction allows the determination of the 3-D structure of metalloproteins and their metal centres. 

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