R
Raymond Behrendt
Researcher at Max Planck Society
Publications - 24
Citations - 1666
Raymond Behrendt is an academic researcher from Max Planck Society. The author has contributed to research in topics: Isomerization & Azobenzene. The author has an hindex of 17, co-authored 24 publications receiving 1606 citations. Previous affiliations of Raymond Behrendt include Goethe University Frankfurt.
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Ultrafast spectroscopy reveals subnanosecond peptide conformational dynamics and validates molecular dynamics simulation
S. Spörlein,Heiko Carstens,Helmut Satzger,Christian Renner,Raymond Behrendt,Luis Moroder,Paul Tavan,Wolfgang Zinth,Josef Wachtveitl +8 more
TL;DR: It is verified that all-atom molecular dynamics simulations can quantitatively describe the subnanosecond conformational dynamics of peptides, strengthening confidence in corresponding predictions for longer time scales.
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Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity
TL;DR: Mouse RNase H2 is essential to remove ribonucleotides from the genome to prevent DNA damage and it is shown that inhibiting this enzyme results in cell death and cell death in mice.
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Transient 2D-IR spectroscopy: Snapshots of the nonequilibrium ensemble during the picosecond conformational transition of a small peptide
Jens Bredenbeck,Jan Helbing,Raymond Behrendt,Christian Renner,Luis Moroder,Josef Wachtveitl,Peter Hamm +6 more
TL;DR: In this article, a cyclic peptide is studied in the amide-I spectral range, which is induced by means of a photoswitch integrated into the peptide backbone and substantial changes are found in the transient 2D-IR spectra at times when the transient 1D spectra show only a minor time dependence.
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Picosecond conformational transition and equilibration of a cyclic peptide
Jens Bredenbeck,Jan Helbing,A. Sieg,Tobias E. Schrader,Wolfgang Zinth,Christian Renner,Raymond Behrendt,Luis Moroder,Josef Wachtveitl,Peter Hamm +9 more
TL;DR: Albeit possessing only a few conformational degrees of freedom compared with a protein, the peptide behaves highly nontrivially and provides insights into the complexity of fast protein folding.
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Mutational studies on HslU and its docking mode with HslV
Hyun Kyu Song,Claudia Hartmann,Ravishankar Ramachandran,Matthias Bochtler,Matthias Bochtler,Raymond Behrendt,Luis Moroder,Robert Huber +7 more
TL;DR: ATP-binding site mutations confirm the essential role of the "sensor arginine" and the "arginine finger" in the ATPase action of HslU and demonstrate an important role for E321, and a better refined structure of the HslVU complex crystallized along with resorufin-labeled casein is reported.