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• A saposin-lipoprotein nanoparticle system for membrane proteins.
• Back Cover: Membrane Chemistry Tunes the Structure of a Peptide Transporter (Angew. Chem. Int. Ed. 43/2020)
• Characterization of the complex of the lysosomal membrane transporter MFSD1 and its accessory subunit GLMP
• Completing the family of human Eps15 homology domains: Solution structure of the internal Eps15 homology domain of γ‐synergin
• Conformational plasticity and dynamics in the generic protein folding catalyst SlyD unraveled by single-molecule FRET.
• Conformational switch upon phosphorylation: human CDK inhibitor p19INK4d between the native and partially folded state.
• Cryo-EM structure of an atypical proton-coupled peptide transporter: Di- and tripeptide permease C
• Crystal structure determination and functional characterization of the metallochaperone SlyD from Thermus thermophilus.
• Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif
• Deamidation drives molecular aging of the SARS-CoV-2 spike receptor-binding motif
• Dissecting the Gene Expression, Localization, Membrane Topology, and Function of the Plasmodium falciparum STEVOR Protein Family
• Escherichia coli peptide binding protein OppA has a preference for positively charged peptides.
• Fast amide proton exchange reveals close relation between native-state dynamics and unfolding kinetics.
• Folding mechanism of an ankyrin repeat protein: scaffold and active site formation of human CDK inhibitor p19(INK4d).
• Front Cover: Single‐Molecule FRET of Membrane Transport Proteins (ChemBioChem 17/2021)
• High-resolution insights into binding of unfolded polypeptides by the PPIase chaperone SlpA.
• High-throughput analytical gel filtration screening of integral membrane proteins for structural studies.
• High-throughput stability screening for detergent-solubilized membrane proteins.
• Identification of novel inner membrane complex and apical annuli proteins of the malaria parasite Plasmodium falciparum
• Identification of novel inner membrane complex and apical annuli proteins of the malaria parasitePlasmodium falciparum
• Identification of three phases in Onconase refolding.
• Impact of distant peptide substrate residues on enzymatic activity of SlyD.
• In‐depth interrogation of protein thermal unfolding data withMoltenProt
• Lipid-like Peptides can Stabilize Integral Membrane Proteins for Biophysical and Structural Studies.
• Membrane Chemistry Tunes the Structure of a Peptide Transporter
• Membrane chemistry tunes the structure of a peptide transporter.
• Metal-mediated crystallization of the xylose transporter XylE from Escherichia coli in three different crystal forms.
• Molecular basis of mRNA transport by a kinesin-1-atypical tropomyosin complex.
• Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
• Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter
• N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum
• N-terminal phosphorylation regulates the activity of Glycogen Synthase Kinase 3 from Plasmodium falciparum.
• NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD.
• Nanobody mediated crystallization of an archeal mechanosensitive channel.
• Optimisation of over-expression in E. coli and biophysical characterisation of human membrane protein synaptogyrin 1.
• PMRT1, a Plasmodium-specific parasite plasma membrane transporter, is essential for asexual and sexual blood stage development.
• Probing the Architecture of a Multi-PDZ Domain Protein: Structure of PDZK1 in Solution
• Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution.
• Rücktitelbild: Membrane Chemistry Tunes the Structure of a Peptide Transporter (Angew. Chem. 43/2020)
• Saposin Lipid Nanoparticles: A Highly Versatile and Modular Tool for Membrane Protein Research.
• Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2
• Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2
• Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2.
• Single‐Molecule FRET of Membrane Transport Proteins
• Slow aromatic ring flips detected despite near-degenerate NMR frequencies of the exchanging nuclei.
• Structural Insights Into PfARO and Characterization of its Interaction With PfAIP
• Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A
• Structural and biophysical characterization of the cytoplasmic domains of human BAP29 and BAP31.
• Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A.
• Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters.
• Structural insights into an equilibrium folding intermediate of an archaeal ankyrin repeat protein.
• Structural insights into substrate recognition in proton-dependent oligopeptide transporters.
• Structural role of essential light chains in the apicomplexan glideosome
• Structural role of essential light chains in the apicomplexan glideosome
• Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes
• Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes
• Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers.
• Structure determination of a major facilitator peptide transporter: Inward facing PepTSt from Streptococcus thermophilus crystallized in space group P3121
• Structure of Prototypic Peptide Transporter DtpA from E. coli in Complex with Valganciclovir Provides Insights into Drug Binding of Human PepT1
• Structure-based stability analysis of an extremely stable dimeric DNA binding protein from Sulfolobus islandicus.
• The conformational distribution of a major facilitator superfamily peptide transporter is modulated by the membrane composition
• The folding pathway of onconase is directed by a conserved intermediate.
• Transient Expression of Recombinant Membrane-eGFP Fusion Proteins in HEK293 Cells.
• Tripeptide binding in a Proton-Dependent Oligopeptide Transporter.
• Understanding transport by the major facilitator superfamily (MFS): structures pave the way.