P
Per-Åke Nygren
Researcher at Royal Institute of Technology
Publications - 167
Citations - 10186
Per-Åke Nygren is an academic researcher from Royal Institute of Technology. The author has contributed to research in topics: Fusion protein & Affinity chromatography. The author has an hindex of 51, co-authored 167 publications receiving 9672 citations. Previous affiliations of Per-Åke Nygren include Centre national de la recherche scientifique & Stockholm University.
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Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain.
TL;DR: Small protein domains, capable of specific binding to different target proteins have been selected using combinatorial approaches and have a secondary structure similar to the native Z domain and have micromolar dissociation constants (KD) for their respective targets.
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Affinity Fusion Strategies for Detection, Purification, and Immobilization of Recombinant Proteins☆
TL;DR: This review focuses on the use of affinity tag fusions for detection, purification, and immobilization of relized in gene fusion systems involving fusion partners suitable for specific detection of expressed fusion proteins.
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Alternative binding proteins: Affibody binding proteins developed from a small three‐helix bundle scaffold
TL;DR: Small size affibody binding proteins, functionally selected from libraries of a small (6 kDa), non‐cysteine three‐helix bundle domain used as a scaffold, are found to be advantageous for the site‐specific introduction of various labels and radionuclide chelators.
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Specific binding of proinsulin C-peptide to human cell membranes
Rudolf Rigler,Aladdin Pramanik,Per Jonasson,Gunnar Kratz,Olof Jansson,Per-Åke Nygren,Stefan Ståhl,Karin Ekberg,Bo-Lennart Johansson,Staffan Uhlén,Mathias Uhlén,Hans Jörnvall,John Wahren +12 more
TL;DR: It is concluded that C-peptide binds to specific G protein-coupled receptors on human cell membranes, thus providing a molecular basis for its biological effects.
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A combinatorial library of an alpha-helical bacterial receptor domain.
TL;DR: Results proved that members of this alpha-helical receptor library with multiple substitutions in the solvent-exposed surface remain stable and soluble in E. coli.