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Friedrich Siebert

Friedrich Siebert

D-Index & Metrics

Chemistry

D-Index
52
Citations
8229
World Ranking
13670
National Ranking
1007

Overview

Friedrich Siebert is affiliated with the University of Freiburg in Germany. Their research spans several interconnected fields, focusing primarily on Agricultural and Biological Sciences, Biochemistry, Genetics and Molecular Biology, and Neuroscience. Within these main fields, their work concentrates on subfields including Plant Science, Molecular Biology, and Cellular and Molecular Neuroscience.

The core topics in Siebert's research revolve around light-related biological processes, specifically:

  • Light effects on plants
  • Photosynthetic Processes and Mechanisms
  • Photoreceptor and optogenetics research

Siebert has published multiple peer-reviewed papers contributing to the understanding of how light influences protein and plant functions. Notable recent papers include:

  • "Intramolecular Proton Transfer Controls Protein Structural Changes in Phytochrome," 2020, published in Biochemistry
  • "Local Electric Field Changes during the Photoconversion of the Bathy Phytochrome Agp2," 2021, published in Biochemistry
  • "Light- and temperature-dependent dynamics of chromophore and protein structural changes in bathy phytochrome Agp2," 2021, published in Physical Chemistry Chemical Physics

These publications reflect a focus on molecular mechanisms underlying photoconversion and protein structural changes in phytochromes, which are light-sensitive proteins involved in plant development and signaling.

Siebert commonly collaborates with a group of co-authors who frequently appear on these papers. The prominent collaborators include:

  • Anastasia Kraskov
  • David Buhrke
  • Norbert Michael
  • Patrick Scheerer
  • Peter Hildebrandt

The publication venues where Siebert's research appears most often tend to be specialized journals in molecular biology and physical chemistry. These include:

  • Biochemistry
  • Physical Chemistry Chemical Physics

Best Publications

  • Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation of static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane

    Engelhard M;Gerwert K;Hess B;Kreutz W

  • Vibrational spectroscopy in life science

    Friedrich Siebert;Peter Hildebrandt

  • Time-Resolved FT-IR Absorption Spectroscopy Using a Step-Scan Interferometer

    Wolfgang Uhmann;Andreas Becker;Christoph Taran;Friedrich Siebert

  • Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: a Fourier-transform infrared spectroscopy study of site-directed mutants.

    Karim Fahmy;Frank Jager;Mareike Beck;Tatyana A. Zvyaga

  • Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals.

    Klaus Gerwert;Friedrich Siebert

  • Functional role of the "ionic lock"--an interhelical hydrogen-bond network in family A heptahelical receptors.

    Reiner Vogel;Mohana Mahalingam;Steffen Lüdeke;Thomas Huber

  • Investigation of the Primary Photochemistry of Bacteriorhodopsin by Low‐Temperature Fourier‐Transform Infrared Spectroscopy

    Friedrich Siebert;Werner Mäntele

  • Identification of Glutamic Acid 113 as the Schiff Base Proton Acceptor in the Metarhodopsin II Photointermediate of Rhodopsin

    Jäger F;Fahmy K;Sakmar Tp;Siebert F

  • The Amino Terminus of the Fourth Cytoplasmic Loop of Rhodopsin Modulates Rhodopsin-Transducin Interaction

    Ethan P. Marin;A.Gopala Krishna;Tatyana A. Zvyaga;Juergen Isele

  • Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation.

    Gu¨nther Metz;Friedrich Siebert;Martin Engelhard

  • Removal of the 9-methyl group of retinal inhibits signal transduction in the visual process. A Fourier transform infrared and biochemical investigation.

    Ulrich M. Ganter;Eduard D. Schmid;Dolores Perez-Sala;Robert R. Rando

  • Evidence for the protonation of two internal carboxylic groups during the photocycle of bacteriorhodopsin: Investigation of kinetic infrared spectroscopy

    F. Siebert;W. Mäntele;W. Kreutz

  • Charge transfer in peptides: Intramolecular radical transformations involving methionine, tryptophan and tyrosine

    Walter A. Prütz;Fritz Siebert;John Butler;Edward J. Land

  • Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy.

    X. Jiang;E. Zaitseva;M. Schmidt;F. Siebert

  • Conformations of the Active and Inactive States of Opsin

    Reiner Vogel;Friedrich Siebert

  • Time-Resolved Step-Scan FT-IR Investigations of the Transition from KL to L in the Bacteriorhodopsin Photocycle: Identification of Chromophore Twists by Assigning Hydrogen-Out-Of-Plane (HOOP) Bending Vibrations

    Olaf Weidlich;Friedrich Siebert

  • Fourier-transform infrared spectroscopy applied to rhodopsin. The problem of the protonation state of the retinylidene Schiff base re-investigated.

    Friedrich Siebert;Werner Mäntele;Klaus Gerwert

  • The role of Glu181 in the photoactivation of rhodopsin

    Steffen Lüdeke;Mareike Beck;Elsa C.Y. Yan;Thomas P. Sakmar

  • Vibrational spectroscopy as a tool for probing protein function.

    Reiner Vogel;Friedrich Siebert

  • Time-Resolved Step-Scan Fourier Transform Infrared Spectroscopy Reveals Differences between Early and Late M Intermediates of Bacteriorhodopsin

    C. Rödig;I. Chizhov;O. Weidlich;F. Siebert

  • Infrared spectroscopy applied to biochemical and biological problems.

    Unknown

Frequent Co-Authors

Thomas P. Sakmar
Thomas P. Sakmar Rockefeller University
Martin Engelhard
Martin Engelhard Max Planck Society
Peter Hildebrandt
Peter Hildebrandt Technical University of Berlin
Mordechai Sheves
Mordechai Sheves Weizmann Institute of Science
Wolfgang Gärtner
Wolfgang Gärtner Leipzig University
Hugo Scheer
Hugo Scheer Ludwig-Maximilians-Universität München
Oliver Lenz
Oliver Lenz Johnson & Johnson
Benno Hess
Benno Hess Max Planck Society
Friedhelm Lendzian
Friedhelm Lendzian Technical University of Berlin
Dieter Oesterhelt
Dieter Oesterhelt Max Planck Society

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