共查询到20条相似文献,搜索用时 15 毫秒
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Christian Wasmer Laura Benkemoun Dr. Raimon Sabaté Dr. Michel O. Steinmetz Dr. Bénédicte Coulary‐Salin Dr. Lei Wang Dr. Roland Riek Prof. Sven J. Saupe Dr. Beat H. Meier Prof. 《Angewandte Chemie (International ed. in English)》2009,48(26):4858-4860
Protein deposition frequently occurs as inclusion bodies (IBs) during heterologous protein expression in E. coli. The structure of these E. coli IBs of the prion‐forming domain from the fungal prion HET‐s is the same as that previously determined for fibrils assembled in vitro, and show prion infectivity. These results demonstrate that the IBs of HET‐s(218–289) are amyloids.
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Dr. Juliane Adler Monika Baumann Bruno Voigt Dr. Holger A. Scheidt Dr. Debanjan Bhowmik Dr. Tilmann Häupl Prof. Dr. Bernd Abel Prof. Dr. Perunthiruthy K. Madhu Prof. Dr. Jochen Balbach Prof. Dr. Sudipta Maiti Prof. Dr. Daniel Huster 《Chemphyschem》2016,17(17):2744-2753
A small library of rationally designed amyloid β [Aβ(1–40)] peptide variants is generated, and the morphology of their fibrils is studied. In these molecules, the structurally important hydrophobic contact between phenylalanine 19 (F19) and leucine 34 (L34) is systematically mutated to introduce defined physical forces to act as specific internal constraints on amyloid formation. This Aβ(1–40) peptide library is used to study the fibril morphology of these variants by employing a comprehensive set of biophysical techniques including solution and solid‐state NMR spectroscopy, AFM, fluorescence correlation spectroscopy, and XRD. Overall, the findings demonstrate that the introduction of significant local physical perturbations of a crucial early folding contact of Aβ(1–40) only results in minor alterations of the fibrillar morphology. The thermodynamically stable structure of mature Aβ fibrils proves to be relatively robust against the introduction of significantly altered molecular interaction patterns due to point mutations. This underlines that amyloid fibril formation is a highly generic process in protein misfolding that results in the formation of the thermodynamically most stable cross‐β structure. 相似文献
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In a search for improved resolution of hydrogen/deuterium (H/D) exchange experiments analyzed by mass spectrometry (HXMS), we evaluated two methodologies for a detailed structural study of solvent accessibility in the case of the HET-s(218-295) prion protein. For the first approach, after incubation in the deuterated solvent, aggregated HET-s(218-295) was digested with pepsin and the generated peptides were analyzed by nanospray mass spectrometry in an ion trap, with and without collision-induced dissociation (CID). We compared deuterium incorporation in peptides as determined on peptide pseudomolecular ions and on b and y fragments produced by longer peptides under CID conditions. For both b and y fragment ions, an extensive H/D scrambling phenomenon was observed, in contrast with previous studies comparing CID-MS experiments and (1)H NMR data. Thus, the spatial resolution of HXMS experiments could not be improved by means of MS/MS data generated by an ion trap mass spectrometer. In a second approach, the incorporation of deuterium was analyzed by MS for 76 peptides of the HET-s(218-289) peptide mass fingerprint, and the use of shared boundaries among peptic peptides allowed us to determine deuteration levels of small regions ranging from one to four amino acids. This methodology led to evidence of highly protected regions along the HET-s(218-295) sequence. 相似文献
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Site‐Specific Isotope‐Labeling of Inosine Phosphoramidites and NMR Analysis of an Inosine‐Containing RNA Duplex 下载免费PDF全文
Dr. Andre Dallmann Dr. Alexander V. Beribisky Dr. Felix Gnerlich Martin Rübbelke Dr. Stefan Schiesser Prof. Dr. Thomas Carell Prof. Dr. Michael Sattler 《Chemistry (Weinheim an der Bergstrasse, Germany)》2016,22(43):15350-15359
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Dr. Linda Cerofolini Stefano Giuntini Dr. Azzurra Carlon Dr. Enrico Ravera Dr. Vito Calderone Prof. Marco Fragai Prof. Giacomo Parigi Prof. Claudio Luchinat 《Chemistry (Weinheim an der Bergstrasse, Germany)》2019,25(8):1984-1991
Resonance assignment and structural characterization of pharmacologically relevant proteins promise to improve understanding and safety of these proteins by rational design. However, the PEG coating that is used to evade the immune system also causes these molecules to “evade” the standard structural biology methodologies. We here demonstrate that it is possible to obtain the resonance assignment and a reliable structural model of large PEGylated proteins through an integrated approach encompassing NMR and X-ray crystallography. 相似文献
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Jacso T Franks WT Rose H Fink U Broecker J Keller S Oschkinat H Reif B 《Angewandte Chemie (International ed. in English)》2012,51(2):432-435
Membrane proteins in their native cellular membranes are accessible by dynamic nuclear polarization magic angle spinning solid-state NMR spectroscopy without the need of purification and reconstitution (see picture). Dynamic nuclear polarization is essential to achieve the required gain in sensitivity to observe the membrane protein of interest. 相似文献