Nanobody stability engineering by employing the ΔTm shift; a comparison with apparent rate constants of heat-induced aggregation.
Kunz, Patrick
Nanobody stability engineering by employing the ΔTm shift; a comparison with apparent rate constants of heat-induced aggregation. [electronic resource] - Protein engineering, design & selection : PEDS 12 2019 - 241-249 p. digital
Publication Type: Comparative Study; Journal Article
1741-0134
10.1093/protein/gzz017 doi
Animals
Camelus
Hot Temperature
Protein Aggregates
Protein Engineering
Protein Stability
Single-Domain Antibodies--chemistry
Nanobody stability engineering by employing the ΔTm shift; a comparison with apparent rate constants of heat-induced aggregation. [electronic resource] - Protein engineering, design & selection : PEDS 12 2019 - 241-249 p. digital
Publication Type: Comparative Study; Journal Article
1741-0134
10.1093/protein/gzz017 doi
Animals
Camelus
Hot Temperature
Protein Aggregates
Protein Engineering
Protein Stability
Single-Domain Antibodies--chemistry