Polymers spectroscopy, Nucleic acids, Proteins

The underlying physical principles of NMR have been established and are well understood.8 Applications of both solid- and solution-state NMR spectroscopy can be found in many different disciplines. It is routinely used in structural elucidation of organic and inorganic compounds, polymers, and biomolecules (e.g., proteins, nucleic acids, and carbohydrates). Additionally, NMR can be used to study molecular interactions (e.g., protein-protein and protein-ligand), molecular dynamics, and chemical reactions. It has also been used extensively in medical research and imaging (magnetic resonance imaging). 

The object of NMR spectroscopy on proteins, nucleic acids and other complex polymers is to obtain information on their structure and dynamics. Assignment of individual spectral lines discussed in the preceding section is a prerequisite to one s ability to decipher this information. Actually to do so it is also necessary to understand the nature of the structural and dynamic information inherent in each feature of the spectrum. And one is rightfully asked is the nature of this information such that the result will be worth the labor required to obtain a significant set of assignments An important part of the answer to this question is that NMR is the ONLY physical method which can provide any information at essentially atomic resolution on the structure and dynamics of macromolecules in solution, as well as in the solid state. Whatever the limits of this information, it is better than none. Knowledge of these limits, as well as of the nature of spectroscopic information, is nevertheless necessary, both to realize expectations and to avoid conclusions that go beyond the capabilities of the method. The information content and its limits can be meaningfully discussed for each measured parameter separately, and the common features summarized at the end. 

In recent years, circular dichroism spectroscopy has been widely applied in investigations concerning the molecular structure of chiral polymers. It is a powerful tool for revealing the secondary structures of biological macromolecules, for instance of polypeptides, proteins, and nucleic acids in solution. An... 

No two instructors teach organic chemistry exactly the same way. This book covers all the fundamental topics in detail, building each new concept on those that come before. Many topics may be given more or less emphasis at the discretion of the instructor. Examples of these topics are C NMR spectroscopy, ultraviolet spectroscopy, conservation of orbital symmetiy, amino acids and proteins, nucleic acids, and the special topics chapters, lipids and synthetic polymers. 

Conformations and structures of polymers and biopolymers are accessible by ECD, VCD, and ROA spectroscopy. Suitable chromophores for the ECD are aromatic amino acids, the bases of nucleic acids, and the peptide bonds in the spectral region 270nm and from 230 down to 160nm. The determination of the a-helix content of proteins was... 

Based on work at the Max Planck Institute for Polymer Research [172, 173], pulsed electron paramagnetic resonance (EPR) has experienced a remarkable revival worldwide [174]. In particular, pulsed double electron-electron resonance (DEER) spectroscopy in combination with site-directed spin labeling [175] is extensively used today in studies of the structure of proteins, including their function as carriers of small molecules, and of nucleic acids. Moreover, it is used to probe large, complex biomacromolecules and their assemblies as weU as 1361 protein folding [176]. 

See also Biochemical Applications of Raman Spectroscopy Biomacromolecular Applications of Circular Dichroism and ORD Carbohydrates Studied by NMR Circularly Polarized Luminescence and Fluorescence Detected Circular Dichroism Induced Circular Dichroism Magnetic Circular Dichroism, Theory Nucleic Acids and Nucleotides Studied Using Mass Spectrometry Organometallics Studied Using Mass Spectrometry Polymer Applications of IR and Raman Spectroscopy Proteins Studied Using NMR Spectroscopy Vibrational CD Spectrometers Vibrational CD, Theory. 

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