His primary areas of investigation include Crystallography, Nuclear magnetic resonance spectroscopy, Stereochemistry, Antifreeze protein and Peptide. His Crystallography research includes themes of Calcium-activated potassium channel, Potassium channel, KvLQT1 and Sudden death. His work focuses on many connections between Nuclear magnetic resonance spectroscopy and other disciplines, such as Analytical chemistry, that overlap with his field of interest in Carbon-13 NMR.
The Stereochemistry study combines topics in areas such as Plasma protein binding, Protein secondary structure, Residue, Protein structure and Side chain. His Antifreeze protein research includes elements of Antiparallel and Molecule. His studies deal with areas such as Tryptophan, Conformational isomerism and Circular dichroism as well as Peptide.
The scientist’s investigation covers issues in Stereochemistry, Crystallography, Nuclear magnetic resonance spectroscopy, Biochemistry and Antifreeze protein. Frank D. Sönnichsen combines subjects such as Residue, Isomerization, Protein secondary structure and Peptide with his study of Stereochemistry. His research in Crystallography intersects with topics in Antiparallel, Molecule and Hydrogen bond.
His Nuclear magnetic resonance spectroscopy study combines topics from a wide range of disciplines, such as Cysteine and Analytical chemistry. His study looks at the intersection of Biochemistry and topics like Biophysics with Epidermal growth factor receptor. His Protein structure research incorporates elements of Integral membrane protein, Plasma protein binding and Circular dichroism.
Frank D. Sönnichsen mainly investigates Molecule, Photochemistry, Stereochemistry, Nuclear magnetic resonance and Spin isomers of hydrogen. His biological study spans a wide range of topics, including Intersystem crossing and Powder diffraction. His Stereochemistry study integrates concerns from other disciplines, such as Asteraceae, Cichorieae, Jasmonic acid, Lamiaceae and Derivative.
His work in the fields of Proton NMR overlaps with other areas such as Laser linewidth, Stimulated emission and Background suppression. His Diamagnetism research spans across into areas like Nuclear magnetic resonance spectroscopy and Crystallography. His studies in Crystallography integrate themes in fields like Cover and Density functional theory.
His main research concerns Photochemistry, Proton NMR, Spin isomers of hydrogen, Hyperpolarization and Induced polarization. The concepts of his Photochemistry study are interwoven with issues in Metastability and Nitrogen. His Proton NMR study improves the overall literature in Nuclear magnetic resonance.
His study deals with a combination of Spin isomers of hydrogen and Nuclear magnetic resonance spectroscopy.
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Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
F. D. Sonnichsen;J. E. Van Eyk;R. S. Hodges;B. D. Sykes.
Magnetic Bistability of Molecules in Homogeneous Solution at Room Temperature
S. Venkataramani;U. Jana;M. Dommaschk;F. D. Sönnichsen.
Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure
Nathan J. Cobb;Frank D. Sönnichsen;Hassane Mchaourab;Witold K. Surewicz.
Proceedings of the National Academy of Sciences of the United States of America (2007)
Solution NMR of membrane proteins: practice and challenges.
Charles R. Sanders;Frank Sönnichsen.
Magnetic Resonance in Chemistry (2006)
A diminished role for hydrogen bonds in antifreeze protein binding to ice.
Heman Chao;Michael E. Houston;Robert S. Hodges;Cyril M. Kay.
Solution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase
Wade D. Van Horn;Hak Jun Kim;Charles D. Ellis;Arina Hadziselimovic.
Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction.
Frank D Sönnichsen;Carl I DeLuca;Peter L Davies;Brian D Sykes.
Structure of KCNE1 and Implications for How It Modulates the KCNQ1 Potassium Channel
Congbao Kang;Changlin Tian;Frank D. Sönnichsen;Jarrod A. Smith.
Solution Structure of the E200K Variant of Human Prion Protein IMPLICATIONS FOR THE MECHANISM OF PATHOGENESIS IN FAMILIAL PRION DISEASES
Yongbo Zhang;Wieslaw Swietnicki;Michael G. Zagorski;Witold K. Surewicz.
Journal of Biological Chemistry (2000)
Structure‐function relationship in the globular type III antifreeze protein: Identification of a cluster of surface residues required for binding to ice
Heman Chao;Carl I. DeLuca;Peter L. Davies;Brian D. Sykes.
Protein Science (1994)
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