Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Marion Haensler"'
Autor:
Johannes-Dieter Wissmann, Sebastian W. Kirbach, Marion Haensler, Frank Bordusa, Nicole Wehofsky
Publikováno v:
Tetrahedron: Asymmetry. 11:2421-2428
The effect of freezing on the enzymatic coupling of highly specific amino acid-containing peptide fragments was investigated using trypsin, α-chymotrypsin, and Bacillus licheniformis Glu-specific endopeptidase as biocatalysts. Comparison with reacti
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 9:91-95
The internal structure of a protease-catalyzed frozen aqueous peptide synthesis system was studied by freeze-fracture electron microscopy. Distinct lense-like liquid microinclusions differing in size from 0.25 to 1.7 μm were observed. Differential s
Publikováno v:
Journal of Peptide Science. 6:366-371
The capability of Glu/Asp-specific endopeptidase from Bacillus licheniformis to form Glu/Asp-Xaa bonds in frozen aqueous systems was investigated. Under frozen state conditions, the enzyme was able to catalyse peptide bond formation more effectively
Publikováno v:
Nucleosides and Nucleotides. 17:1267-1274
Synthesis of guanylyl(3′→5′)cytidine catalysed by RNase T1 variants (Tyr42Trp, Tyr24Trp and GluSSAla) was studied in frozen aqueous systems at-10°C and in solution at 0°C. Freezing the reaction mixture resulted in significantly enhanced dinuc
Autor:
Hans-Dieter Jakubke, Marion Haensler
Publikováno v:
Enzyme and Microbial Technology. 22:617-620
The capability of endoproteinase Pro-C from Flavobacterium meningosepticum to form peptide bonds in frozen aqueous systems was investigated. In coupling of Bz-Gly-Pro-OMe with various amino acid amides, free amino acids, and dipeptides, freezing-indu
Publikováno v:
Journal of Chemical Technology & Biotechnology. 68:202-208
In order to combine the high potential of frozen state peptide synthesis and the advantages of the application of immobilized proteases, the capability of carrier-bound α-chymotrypsin (CT, EC 3.4.21.1) to form peptide bonds in frozen aqueous reactio
Autor:
Frank Bordusa, Nicole Wehofsky, Johannes-Dieter Wissmann, Marion Haensler, Sebastian W. Kirbach
Publikováno v:
Organic letters. 2(14)
[reaction: see text] We present an irreversible and efficient protease-based method for peptide synthesis which occurs independently of the primary specificity of proteases and also without proteolytic side reactions. The key feature of this approach
Autor:
Marion Haensler, Klaus Arnold
Publikováno v:
Biological chemistry. 381(1)
In order to investigate the effect of freezing on aqueous protease-catalyzed peptide synthesis systems, the influence of polyethylene glycols as cryoprotecting substances on α-chymotrypsin-catalyzed coupling of a N-protected acyl donor ester and var
Publikováno v:
Biochemistry. 38(4)
Attempts to modify the guanine specificity of ribonuclease T1 (RNase T1) by rationally designed amino acid substitutions failed so far. Therefore, we applied a semirational approach by randomizing the guanine binding site. A combinatorial library of