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Gruppiere nach: Keine Gruppierung | Typ des Eintrags | Publikationsjahr | Sprache
Springe zu: 1998 | 1997 | 1996 | 1995
Anzahl der Einträge: 8.

1998

Putlitz, J. zu ; Skerra, ; Schroder, ; Zentgraf, ; Wands, (1998)
Cloning, bacterial synthesis, and characterization of immunoglobulin variable regions of a monoclonal antibody specific for the hepatitis B virus X protein.
In: Gene. 221 (1998), S. 143-149
Artikel, Bibliographie

König, T. ; Skerra, (1998)
Use of an albumin-binding domain for the selective immobilisation of recombinant capture antibody fragments of ELISA plates.
In: Journal of immunological methods. 218 (1998), S. 73-83
Artikel, Bibliographie

1997

Steipe, B. ; Skerra, (1997)
Das grün fluoreszierende Protein.
In: BIOspektrum. 1997, 1, S. 28-30
Artikel, Bibliographie

Tudyka, Tatjana ; Skerra, (1997)
Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli.
In: Protein science. 6 (1997), S. 2180-2187
Artikel, Bibliographie

Voss, Selma ; Skerra, (1997)
Mutagenesis of a flexible loop in streptavidin leads to higher affinity for the Strep-tag II peptide and improved performance in recombinant protein purification.
In: Protein engineering. 10 (1997), S. 975-982
Artikel, Bibliographie

Schieweck, Wolfram ; Skerra, (1997)
The rational construction of an antibody against cystatin: lessons from the crystal structure of an artificial F ab fragment.
In: Journal of molecular biology. 268 (1997), S. 934-951
Artikel, Bibliographie

1996

Schmidt, A. M. ; Müller, ; Skerra, (1996)
A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand.
In: Chemistry and biology. 3 (1996), S. 645-653
Artikel, Bibliographie

1995

Schieweck, W. ; Skerra, (1995)
Fermenter production of an artificial Fab fragment, rationally designed for the antigen cystatin, and its optimized crystallization through constant domain shuffling.
In: Proteins. 23 (1995), S. 561-565
Artikel, Bibliographie

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