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Investigation of the structure of a model iron-sulfur protein by spin and luminescence label methods. 1972

G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D008163 Luminescent Measurements Techniques used for determining the values of photometric parameters of light resulting from LUMINESCENCE. Bioluminescence Measurements,Bioluminescent Assays,Bioluminescent Measurements,Chemiluminescence Measurements,Chemiluminescent Assays,Chemiluminescent Measurements,Chemoluminescence Measurements,Luminescence Measurements,Luminescent Assays,Luminescent Techniques,Phosphorescence Measurements,Phosphorescent Assays,Phosphorescent Measurements,Assay, Bioluminescent,Assay, Chemiluminescent,Assay, Luminescent,Assay, Phosphorescent,Assays, Bioluminescent,Assays, Chemiluminescent,Assays, Luminescent,Assays, Phosphorescent,Bioluminescence Measurement,Bioluminescent Assay,Bioluminescent Measurement,Chemiluminescence Measurement,Chemiluminescent Assay,Chemiluminescent Measurement,Chemoluminescence Measurement,Luminescence Measurement,Luminescent Assay,Luminescent Measurement,Luminescent Technique,Measurement, Bioluminescence,Measurement, Bioluminescent,Measurement, Chemiluminescence,Measurement, Chemiluminescent,Measurement, Chemoluminescence,Measurement, Luminescence,Measurement, Luminescent,Measurement, Phosphorescence,Measurement, Phosphorescent,Measurements, Bioluminescence,Measurements, Bioluminescent,Measurements, Chemiluminescence,Measurements, Chemiluminescent,Measurements, Chemoluminescence,Measurements, Luminescence,Measurements, Luminescent,Measurements, Phosphorescence,Measurements, Phosphorescent,Phosphorescence Measurement,Phosphorescent Assay,Phosphorescent Measurement,Technique, Luminescent,Techniques, Luminescent
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D008956 Models, Chemical Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment. Chemical Models,Chemical Model,Model, Chemical
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002499 Centrifugation, Density Gradient Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Centrifugations, Density Gradient,Density Gradient Centrifugation,Density Gradient Centrifugations,Gradient Centrifugation, Density,Gradient Centrifugations, Density
D002621 Chemistry A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
D002729 Chloromercuribenzoates Chloride and mercury-containing derivatives of benzoic acid.

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G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
A spin label investigation of some model membrane systems.
November 1972, Chemistry and physics of lipids,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
Iron-sulfur proteins: spin-coupling model for three-iron clusters.
November 1980, Proceedings of the National Academy of Sciences of the United States of America,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
[Model molybdenum-sulfur and molybdenum-iron-sulfur protein complexes].
December 1996, Bioorganicheskaia khimiia,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
Investigation of iron-sulfur protein maturation in eukaryotes.
January 2007, Methods in molecular biology (Clifton, N.J.),
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Characterization of Weak Protein Domain Structure by Spin-Label Distance Distributions.
January 2021, Frontiers in molecular biosciences,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
[Characterization of dynamic behavior of side groups of globular proteins by spin-label, NMR and luminescence polarization methods].
January 1983, Molekuliarnaia biologiia,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
Studies on the spin-spin interaction between flavin and iron-sulfur cluster in an iron-sulfur flavoprotein.
January 1986, Biochimica et biophysica acta,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
Electronic structure investigation and parametrization of biologically relevant iron-sulfur clusters.
February 2014, Journal of chemical information and modeling,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
The primary structure of Chromatium high-potential iron-sulfur protein.
June 1971, Biochemical and biophysical research communications,
G I Likhtenshtein, and E N Frolov, and N F Neznaikov, and L A Levchenko, and Y S Sklyar
Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD.
September 2003, Acta crystallographica. Section D, Biological crystallography,
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