Results 301 to 310 of about 323,420 (331)

CryoWriter: A Robotic Solution for Improved Cryo-EM Grid Preparation

Chinmaya K, Ekundayo B, Di Fabrizio M, Mohammed I, Radecke J, Stahlberg H, Kube M.   +6 more
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Switchable reinforced streptavidin

Nanoscale, 2020
Introducing a disulfide bridge within monovalent streptavidin's N-terminal β-sheet structure significantly increases the mechanical stability of the biotin/streptavidin complex.
Leonard C. Schendel, Steffen M. Sedlak, Hermann E. Gaub   +2 more
openaire   +2 more sources

Autodisplay of streptavidin

Enzyme and Microbial Technology, 2011
Streptavidin was expressed on the outer membrane of E. coli as a recombinant fusion protein with an autotransporter domain called AIDA-I (adhesin involved in diffuse adherence) using autodisplay technology. The autodisplay of streptavidin was confirmed by SDS-PAGE of the outer membrane proteins, and the number of autodisplayed streptavidin molecules on
Min, Park, Joachim, Jose, Sarah, Thömmes, Jo-Il, Kim, Min-Jung, Kang, Jae-Chul, Pyun   +5 more
openaire   +2 more sources

Smart Polymer–Streptavidin Conjugates

ChemInform, 2004
AbstractFor Abstract see ChemInform Abstract in Full Text.
Patrick S, Stayton, Zhongli, Ding, Allan S, Hoffman   +2 more
openaire   +2 more sources

Streptavidin in Antibody Pretargeting. Comparison of a Recombinant Streptavidin with Two Streptavidin Mutant Proteins and Two Commercially Available Streptavidin Proteins

Bioconjugate Chemistry, 1998
In this investigation, a comparison of wild type recombinant streptavidin (r-SAv) with two genetically engineered mutant r-SAv proteins was undertaken. The investigation also included a comparison of the r-SAv with two streptavidin (SAv) proteins from commercial sources. In vitro characterization of the SAv proteins was conducted by HPLC, SDS-PAGE, IEF,
D S, Wilbur, P S, Stayton, R, To, K R, Buhler, L A, Klumb, D K, Hamlin, J E, Stray, R L, Vessella   +7 more
openaire   +2 more sources

Smart and biofunctional streptavidin

Biomolecular Engineering, 1999
The high affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. While it is extremely useful as the native protein, there are many applications where its function can be improved re-engineering the subunits.
P S, Stayton, K E, Nelson, T C, McDevitt, V, Bulmus, T, Shimoboji, Z, Ding, A S, Hoffman   +6 more
openaire   +2 more sources

Streptavidin–biotin binding energetics

Biomolecular Engineering, 1999
The high affinity energetics in the streptavidin-biotin system provide an excellent model system for studying how proteins balance enthalpic and entropic components to generate an impressive overall free energy for ligand binding. We review here concerted site-directed mutagenesis, biophysical, and computational studies of aromatic and hydrogen bonding
P S, Stayton, S, Freitag, L A, Klumb, A, Chilkoti, V, Chu, J E, Penzotti, R, To, D, Hyre, I, Le Trong, T P, Lybrand, R E, Stenkamp   +10 more
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Protein engineering of streptavidin for in vivo assembly of streptavidin beads

Journal of Biotechnology, 2008
Escherichia coli was engineered to intracellularly manufacture streptavidin beads. Variants of streptavidin (monomeric, core and mature full length streptavidin) were C-terminally fused to PhaC, the polyester granule forming enzyme of Cupriavidus necator. All streptavidin fusion proteins mediated formation of the respective granules in E. coli and were
Peters, Verena, Rehm, Bernd HA
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Oligonucleotide-Blocked Streptavidin for Biotinylation Analysis

Bioconjugate Chemistry, 2022
Binding between streptavidin, or its homologues, to biotin is one of the most widely exploited biological interactions in the biomedical sciences. Controlling the extent of biotinylation is important for meeting the requirements of the intended design and to preserve the native function of the biotin recipient.
Steven K. Taylor, Natasa Kostic, Milan N. Stojanovic   +2 more
openaire   +2 more sources