Medizinische Universität Graz - Research portal
Selected Publication:
Jermutus, L; Kolly, R; Földes-Papp, Z; Hanes, J; Rigler, R; Plückthun, A.
Ligand binding of a ribosome-displayed protein detected in solution at the single molecule level by fluorescence correlation spectroscopy.
Eur Biophys J. 2002; 31(3): 179-184.
Doi: 10.1007/s00249-001-0204-0
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- Co-authors Med Uni Graz
- Földes-Papp Zeno
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- Abstract:
- Interaction of a single-chain antibody fragment (scFv) with its cognate antigen while still attached to the ribosome was studied by fluorescence correlation spectroscopy (FCS). In experiments with purified scFv, FCS was capable of resolving the difference in diffusion time between free and antibody-bound labelled antigen. Ribosome-displayed antibody fragments generated by in vitro translation, in which neither the protein nor the mRNA leaves the ribosome owing to the absence of a stop codon and stabilizing buffer conditions, could be shown to specifically bind the antigen. The antibody-antigen interaction was specific, as shown by inhibition or displacement with unlabelled antigen and by control experiments with a non-cognate antibody fragment.
- Find related publications in this database (using NLM MeSH Indexing)
- Amino Acid Sequence -
- Antibodies, Monoclonal -
- Antigen-Antibody Complex - chemistry
- Antigen-Antibody Reactions - chemistry
- Immunoglobulin Fragments - chemistry
- Immunoglobulin Variable Region - chemistry
- Ligands - chemistry
- Macromolecular Substances - chemistry
- Microscopy, Fluorescence - methods
- Molecular Sequence Data - methods
- Nanotechnology - methods
- Protein Interaction Mapping - methods
- Ribosomal Proteins - chemistry
- Sensitivity and Specificity - chemistry
- Find related publications in this database (Keywords)
- fluorescence correlation spectroscopy
- single molecule analysis
- ribosome display
- single-chain antibody fragment
- scFv