A5028476493- RNA and protein synthesis mechanisms
- RNA modifications and cancer
- RNA Research and Splicing
- Bacterial Genetics and Biotechnology
- Bacteriophages and microbial interactions
- DNA and Nucleic Acid Chemistry
- Viral Infections and Immunology Research
- Peptidase Inhibition and Analysis
- Genomics and Phylogenetic Studies
- Enzyme Structure and Function
- Toxin Mechanisms and Immunotoxins
- Medical Imaging and Pathology Studies
- Protein Structure and Dynamics
- Particle accelerators and beam dynamics
- Chemical Synthesis and Analysis
- Biochemical and Molecular Research
- Radiopharmaceutical Chemistry and Applications
- Antimicrobial Peptides and Activities
- Advanced biosensing and bioanalysis techniques
- Cancer-related gene regulation
- Monoclonal and Polyclonal Antibodies Research
- CRISPR and Genetic Engineering
- Cancer-related molecular mechanisms research
- Mass Spectrometry Techniques and Applications
- HIV Research and Treatment
Max Planck Institute for Multidisciplinary Sciences
2022-2024
Tissue Dynamics (Israel)
2024
Max Planck Institute for Biophysical Chemistry
2013-2022
Max Planck Institute for the Study of Religious and Ethnic Diversity
2022
Nanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103
2021
Multiscale Bioimaging
2020-2021
University of Göttingen
2020
Wake Forest University
2017
Max Planck Society
2006-2015
Witten/Herdecke University
2002-2014
Elongation factor P (EF-P) is a translation of unknown function that has been implicated in great variety cellular processes. Here, we show EF-P prevents ribosome from stalling during synthesis proteins containing consecutive prolines, such as PPG, PPP, or longer proline strings, natural and engineered model proteins. promotes peptide-bond formation stabilizes the peptidyl-transfer RNA catalytic center ribosome. posttranslationally modified by hydroxylated β-lysine attached to lysine...
Article6 August 2016Open Access NSUN3 and ABH1 modify the wobble position of mt-tRNAMet to expand codon recognition in mitochondrial translation Sara Haag Institute for Molecular Biology, University Medical Center Göttingen, Georg-August-University, Germany Search more papers by this author Katherine E Sloan Namit Ranjan Department Physical Biochemistry, Max Planck Biophysical Chemistry, Ahmed S Warda Jens Kretschmer Charlotte Blessing Benedikt Hübner Jan Seikowski Organic Biomolecular Sven...
Protein domains can fold into stable tertiary structures while they are synthesized on the ribosome. We used a high-performance, reconstituted in vitro translation system to investigate folding of small five-helix protein domain-the N-terminal domain Escherichia coli N5-glutamine methyltransferase HemK-in real time. Our observations show that cotranslational protein, which folds autonomously and rapidly solution, proceeds through compact, non-native conformation forms within peptide tunnel...
To determine the effectiveness of ribosome as a catalyst, we compared rate uncatalyzed peptide bond formation, by reaction ethylene glycol ester N -formylglycine with Tris(hydroxymethyl)aminomethane, peptidyl transfer ribosome. Activation parameters were also determined for both reactions, from temperature dependence their second-order constants. In contrast most protein enzymes, enthalpy activation is slightly less favorable on than in solution. The 2 × 10 7 -fold enhancement produced...
The stoichiometry of elongation factor Tu (EF-Tu) and GTP in the complex with aminoacyl-tRNA consumption during peptide bond formation on ribosome were studied Escherichia coli system. ribosomes programmed either two different heteropolymeric mRNAs coding for Met-Phe-Thr-Ile ... (mMFTI) or Met-Phe-Phe-Gly (mMFFG) poly(U). composition EF-Tu, GTP, Phe-tRNA(Phe) was by gel chromatography. With equimolar amounts Phe-tRNA(Phe), a pentameric complex, (EF-Tu.GTP)2.Phe-tRNA(Phe), observed, whereas...