Thorsten Dieckmann

ORCID: 0000-0002-1360-3199
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About
Contact & Profiles
Research Areas
  • RNA and protein synthesis mechanisms
  • DNA and Nucleic Acid Chemistry
  • RNA modifications and cancer
  • Advanced biosensing and bioanalysis techniques
  • Bacteriophages and microbial interactions
  • RNA Research and Splicing
  • Electron Spin Resonance Studies
  • Various Chemistry Research Topics
  • Nitric Oxide and Endothelin Effects
  • Protein Structure and Dynamics
  • Advanced NMR Techniques and Applications
  • Chemical Synthesis and Analysis
  • Hemoglobin structure and function
  • Genomics and Phylogenetic Studies
  • Molecular spectroscopy and chirality
  • Photoreceptor and optogenetics research
  • Bacterial Genetics and Biotechnology
  • Physiological and biochemical adaptations
  • RNA Interference and Gene Delivery
  • Glycosylation and Glycoproteins Research
  • NMR spectroscopy and applications
  • Biochemical and Molecular Research
  • Photosynthetic Processes and Mechanisms
  • Peptidase Inhibition and Analysis
  • Diverse Educational Innovations Studies

University of Waterloo
2014-2024

University of California, Davis
2001-2004

Harvard University
2003

University of California, Merced
2003

University of California, Los Angeles
1994-2001

Institut de Pharmacologie et de Biologie Structurale
2001

University of California System
2001

European Molecular Biology Laboratory
1994

European Molecular Biology Laboratory
1994

Ludwig-Maximilians-Universität München
1993

Abstract Ribonucleic acids are an attractive drug target owing to their central role in many pathological processes. Notwithstanding this potential, RNA has only rarely been successfully targeted with novel drugs. The difficulty of targeting is at least part due the unusual mode binding found most small‐molecule–RNA complexes: ligand pocket largely unstructured absence and forms a defined structure acting as scaffold for folding. Moreover, electrostatic interactions between can also induce...

10.1002/cbic.200300701 article EN ChemBioChem 2003-12-19

The structure of human parathyroid hormone fragment (1-34) in a solvent mixture water and trifluoroethanol has been determined by 1H nuclear magnetic resonance spectroscopy combination distance geometry molecular dynamic simulations. After complete assignment the signals, Overhauser enhancement data imply existence two alpha-helices, comprising residues 3-9 17-28, joined nonstructured region. absence any long-range NOEs relative magnitudes sequential 3J(HNH alpha) values reflect an inherent...

10.1021/bi00242a018 article EN Biochemistry 1991-07-01

AbstractThe CGG triplet repeat found within the 5'UTR of FMR1 gene is involved in pathogenesis both fragile X syndrome and X-associated tremor/ataxia (FXTAS). The has been shown to form hairpins tetraplexes DNA; however, secondary structure CGG-repeat RNA not well defined. To this end, we have performed NMR spectroscopy on vitro transcribed RNAs see clear evidence intramolecular hairpins, with no tetraplex structures. Both C•G G◦G base pairs hairpin stem, though a dynamic equilibrium...

10.4161/rna.4.2.5039 article EN RNA Biology 2007-04-01

Calmodulin (CaM) is a cytosolic Ca2+-binding protein that serves as control element for many enzymes. It consists of two globular domains, each containing EF hand pairs capable binding Ca2+, joined by flexible central linker region. CaM able to bind and activate its target proteins in the Ca2+-replete Ca2+-deplete forms. To study Ca2+-dependent/independent properties activation CaM, constructs with disrupting mutations Asp Ala at position one have been used. These mutant are deficient Ca2+...

10.1021/acs.biochem.6b01296 article EN Biochemistry 2017-01-25

Abstract Structural biology has made important contributions to the understanding of biological processes. In recent years an increasing amount structural information also been derived from NMR spectroscopic studies, often with special emphasis on dynamic aspects. The introduction three‐ and four‐dimensional techniques greatly simplified protein structure determination by Spectroscopy, which in fact become routine. past it was more art interpret complicated NOESY spectra proteins, but...

10.1002/anie.199402771 article EN Angewandte Chemie International Edition 1994-02-18

10.1016/j.pnmrs.2006.03.001 article EN Progress in Nuclear Magnetic Resonance Spectroscopy 2006-05-01

Nitric oxide synthase (NOS) plays a major role in number of key physiological and pathological processes. Knowledge how this is regulated important. The small acidic calcium binding protein, calmodulin (CaM), required to fully activate the enzyme. exact mechanism CaM activates NOS not understood. Studies have shown act like switch that causes conformational change allow for transfer an electron between reductase oxygenase domains through process thought be highly dynamic. To investigate...

10.1021/bi300327z article EN Biochemistry 2012-04-09

RNA plays a central role in many biological processes and is therefore an important target for drug development. In recent years increasing wealth of structural functional information about RNA−ligand complexes has been obtained using vitro selected RNAs (aptamers). However, all those studies focused on structure changes the nucleic acid mostly considered ligand as rigid target. To develop detailed picture dynamics RNA−small molecule complexes, malachite green binding aptamer was studied....

10.1021/ja027635d article EN Journal of the American Chemical Society 2002-11-22

Filter-diagonalization [M. R. Wall and D. Neuhauser, J. Chem. Phys. 102, 8011 (1995)] is a new method for extracting frequencies damping constants from short-time segment of any time-dependent signal, whether quantum origin or not. The efficient able to handle signals with, e.g., millions (possibly overlapping) frequencies, since it concentrates on specific spectral ranges. was shown be powerful tool eigenstates normal-modes, reducing propagation times, in several recent works by us,...

10.1063/1.476263 article EN The Journal of Chemical Physics 1998-05-22
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