|
|
|
|
LEADER |
01927 am a22002893u 4500 |
001 |
108551 |
042 |
|
|
|a dc
|
100 |
1 |
0 |
|a Theile, Christopher S.
|e author
|
100 |
1 |
0 |
|a Massachusetts Institute of Technology. Department of Biology
|e contributor
|
100 |
1 |
0 |
|a Whitehead Institute for Biomedical Research
|e contributor
|
100 |
1 |
0 |
|a Ploegh, Hidde
|e contributor
|
700 |
1 |
0 |
|a Chen, Guan-Yu
|e author
|
700 |
1 |
0 |
|a Bilate, Angelina M.
|e author
|
700 |
1 |
0 |
|a Duarte, Joao N.
|e author
|
700 |
1 |
0 |
|a Avalos, Ana M.
|e author
|
700 |
1 |
0 |
|a Fang, Tao
|e author
|
700 |
1 |
0 |
|a Barberena, Roberto
|e author
|
700 |
1 |
0 |
|a Sato, Shuji
|e author
|
700 |
1 |
0 |
|a Ploegh, Hidde
|e author
|
700 |
1 |
0 |
|a Li, Zeyang,S.M.Massachusetts Institute of Technology.
|e author
|
245 |
0 |
0 |
|a Fluorophore-Conjugated Holliday Junctions for Generating Super-Bright Antibodies and Antibody Fragments
|
260 |
|
|
|b Wiley Blackwell,
|c 2017-05-01T18:47:33Z.
|
856 |
|
|
|z Get fulltext
|u http://hdl.handle.net/1721.1/108551
|
520 |
|
|
|a The site-specific modification of proteins with fluorophores can render a protein fluorescent without compromising its function. To avoid self-quenching from multiple fluorophores installed in close proximity, we used Holliday junctions to label proteins site-specifically. Holliday junctions enable modification with multiple fluorophores at reasonably precise spacing. We designed a Holliday junction with three of its four arms modified with a fluorophore of choice and the remaining arm equipped with a dibenzocyclooctyne substituent to render it reactive with an azide-modified fluorescent single-domain antibody fragment or an intact immunoglobulin produced in a sortase-catalyzed reaction. These fluorescent Holliday junctions improve fluorescence yields for both single-domain and full-sized antibodies without deleterious effects on antigen binding.
|
546 |
|
|
|a en_US
|
655 |
7 |
|
|a Article
|
773 |
|
|
|t Angewandte Chemie International Edition
|