Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Jens Hennecke"'
Autor:
Jens Hennecke, Don C. Wiley
Publikováno v:
Journal of Experimental Medicine. 195:571-581
The α/β T cell receptor (TCR) HA1.7 specific for the hemagglutinin (HA) antigen peptide from influenza A virus is HLA-DR1 restricted but cross-reactive for the HA peptide presented by the allo-major histocompatibility complex (MHC) class II molecul
Publikováno v:
Proteins: Structure, Function, and Genetics. 37:253-263
The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and is required for efficient disulfide bond formation in the bacterial periplasm. DsbA contains two tryptophans: W76 and W126. The fluorescence of W76 changes upon reduction of
Publikováno v:
Journal of Molecular Biology. 286:1197-1215
One of the key questions in protein folding is whether polypeptide chains require unique nucleation sites to fold to the native state. In order to identify possible essential polypeptide segments for folding, we have performed a complete circular per
Publikováno v:
Journal of Biological Chemistry. 272:21692-21699
Disulfide oxidoreductases are structurally related proteins that share the thioredoxin fold and a catalytic disulfide bond that is located at the N terminus of an alpha-helix. The different redox potentials of these enzymes varying from -270 mV for t
Publikováno v:
Biochemistry. 36:6391-6400
The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and required for efficient disulfide bond formation in the bacterial periplasm. The enzyme consists of a thioredoxin-like domain and a second, alpha-helical domain which is inser
Publikováno v:
Journal of Biological Chemistry. 272:189-195
The catalytic disulfide bond Cys30-Cys33 of the disulfide oxidoreductase DsbA from Escherichia coli is located at the amino terminus of an alpha-helix, which has a kink caused by insertion of a tripeptide (residues 38-40). The oxidative force of DsbA
Publikováno v:
Journal of molecular biology. 327(1)
Fluorescence resonance energy transfer (FRET) was used to establish a novel in vivo screening system that allows rapid detection of protein folding and protein variants with increased thermodynamic stability in the cytoplasm of Escherichia coli. The
Autor:
Jens, Hennecke, Don C, Wiley
Publikováno v:
The Journal of Experimental Medicine
The alpha/beta T cell receptor (TCR) HA1.7 specific for the hemagglutinin (HA) antigen peptide from influenza A virus is HLA-DR1 restricted but cross-reactive for the HA peptide presented by the allo-major histocompatibility complex (MHC) class II mo
Publikováno v:
Topics in Fluorescence Spectroscopy ISBN: 9780306464515
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7ac47afdf68d9fc33b9e53a64b50568
https://doi.org/10.1007/0-306-47102-7_6
https://doi.org/10.1007/0-306-47102-7_6
Autor:
Don C. Wiley, Jens Hennecke
Publikováno v:
Cell. 104(1)
X-ray crystal structures of αβTCRs bound to MHCI and MHCII molecules with bound antigenic peptides reveals the atomic contacts upon which MHC restricted T cell recognition is based. Very different signals can result from very similar structures and