Nuclear magnetic resonance spectroscop proteins

Stoffel, W., Zierenberg, O., Tunggal, B. D., and Schreiber, E. (1974). Hoppe-Seyler s Z. Physiol. Chem. 355, 1381. 1 3C Nuclear Magnetic Resonance Spectroscopic Studies on Lipid-Protein Interactions in Human High-Density Lipoprotein (HDL) A Model of the IIDL Particle. 

Aside from the direct techniques of X-ray or electron diffraction, the major possible routes to knowledge of three-dimensional protein structure are prediction from the amino acid sequence and analysis of spectroscopic measurements such as circular dichroism, laser Raman spectroscopy, and nuclear magnetic resonance. With the large data base now available of known three-dimensional protein structures, all of these approaches are making considerable progress, and it seems possible that within a few years some combination of noncrystallo-graphic techniques may be capable of correctly determining new protein structures. Because the problem is inherently quite difficult, it will undoubtedly be essential to make the best possible use of all hints available from the known structures. 

These semisynthetic proteins have served as useful tools to investigate and study the role of Ras proteins in the cell, for instance, new insights in the so-called Ras acylation cycle could be obtained as well as solid-state nuclear magnetic resonance (NMR) spectroscopic analysis of the lipidated membrane anchor and proteins became possible. ... 

In fact, a tremendous amount of information is available on the structures of biological macromolecules descriptions of structures of proteins and nucleic acids make up major portions of modern textbooks in biochemistry and molecular biology. The Protein Data Bank and the Nucleic Acid Database are online archives that contain sequence and structural data on thousands of specific molecules and complexes of molecules. This structural information comes from in vitro experiments, with structures inferred from the x-ray diffraction patterns of crystallized molecules, spectroscopic measurements using multi-dimensional nuclear magnetic resonance, and a host of other methodologies. 

Current subject areas covered are Amino Acids, Peptides and Proteins, Carbohydrate Chemistry, Catalysis, Chemical Modelling Applications and Theory, Electron Paramagnetic Resonance, Nuclear Magnetic Resonance, Organometallic Chemistry, Organophosphorus Chemistry, Photochemistry and Spectroscopic Properties of Inorganic and Organometallic Compounds. 

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