2001 - Fellow of the American Association for the Advancement of Science (AAAS)
1975 - Fellow of John Simon Guggenheim Memorial Foundation
Gerd N. La Mar mostly deals with Proton NMR, Heme, Myoglobin, Hemeprotein and Crystallography. Gerd N. La Mar combines subjects such as Biochemistry, Imidazole, Spin, Nuclear magnetic resonance spectroscopy and Horseradish peroxidase with his study of Proton NMR. His Heme research is multidisciplinary, incorporating elements of Lability, Relaxation behavior and Kinetic energy.
Myoglobin is closely attributed to Stereochemistry in his research. His research investigates the connection between Hemeprotein and topics such as Paramagnetism that intersect with issues in Crystal. The concepts of his Crystallography study are interwoven with issues in Pi, Hemin, Ferric, Protein structure and Methyl group.
His primary areas of investigation include Proton NMR, Heme, Stereochemistry, Crystallography and Myoglobin. The Proton NMR study combines topics in areas such as Paramagnetism, Two-dimensional nuclear magnetic resonance spectroscopy, Molecule, Hydrogen bond and Nuclear magnetic resonance spectroscopy. His research investigates the connection between Heme and topics such as Photochemistry that intersect with problems in Nickel.
In his research on the topic of Stereochemistry, Horseradish peroxidase is strongly related with Active site. He interconnects Relaxation, Hyperfine structure, Spin, Ferric and Electronic structure in the investigation of issues within Crystallography. His biological study spans a wide range of topics, including Hemeprotein, Cyanide and Globin.
Gerd N. La Mar mainly investigates Proton NMR, Stereochemistry, Heme, Crystallography and Active site. His Proton NMR study combines topics in areas such as Myoglobin, Paramagnetism, Ligand, Two-dimensional nuclear magnetic resonance spectroscopy and Molecule. He works on Stereochemistry which deals in particular with Nuclear magnetic resonance spectroscopy.
His study in Heme is interdisciplinary in nature, drawing from both Pyrrole, Cyanide and Globin. The concepts of his Crystallography study are interwoven with issues in Relaxation, Hyperfine structure, Electronic structure, Ferredoxin and Hemeprotein. His Hemeprotein research integrates issues from Ferric and Rhodopseudomonas palustris.
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Proton magnetic resonance investigation of antiferromagnetic oxo-bridged ferric dimers and related high-spin monomeric ferric complexes
Gerd N. La Mar;G. R. Eaton;R. H. Holm;F. Ann. Walker.
Journal of the American Chemical Society (1973)
Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein.
Gerd N. La Mar;N.L. Davis;Daniel W. Parish;Kevin M. Smith.
Journal of Molecular Biology (1983)
NMR of Paramagnetic Molecules: Principles and Applications
Gerd N. La Mar;William DeW. Horrocks;Richard Hadley Holm.
(2016)
Solution structural characterization of cyanometmyoglobin: Resonance assignment of heme cavity residues by two-dimensional NMR
S. Donald Emerson;Gerd N. La Mar.
Biochemistry (1990)
Mechanism of autoxidation of iron(II) porphyrins. Detection of a peroxo-bridged iron(III) porphyrin dimer and the mechanism of its thermal decomposition to the oxo-bridged iron(III) porphyrin dimer
Der-Hang Chin;Gerd N. La Mar;Alan L. Balch.
Journal of the American Chemical Society (1980)
Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: evidence for intramolecular reorientation about a heme two-fold axis
Gerd N. La Mar;Hiroo Toi;R. Krishnamoorthi.
Journal of the American Chemical Society (1984)
Oxygenation patterns for iron(II) porphyrins. Peroxo and ferryl (FeIVO) intermediates detected by proton nuclear magnetic resonance spectroscopy during the oxygenation of (tetramesitylporphyrin)iron(II)
Alan L. Balch;Yee Wai Chan;Ru Jen Cheng;Gerd N. La Mar.
Journal of the American Chemical Society (1984)
Proton NMR characterization of the catalytically relevant proximal and distal hydrogen-bonding networks in ligated resting state horseradish peroxidase
V. Thanabal;Jeffrey S. De Ropp;Gerd N. La Mar.
Journal of the American Chemical Society (1988)
High-spin ferrous porphyrin complexes as models for deoxymyoglobin and -hemoglobin. A proton nuclear magnetic resonance study.
Harold Goff;Gerd N. La Mar.
Journal of the American Chemical Society (1977)
Assignment of proximal histidine proton nmr peaks in myoglobin and hemoglobin
Gerd N. La Mar;David L. Budd;Harold Goff.
Biochemical and Biophysical Research Communications (1977)
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