Ontology highlight
ABSTRACT:
SUBMITTER: Howarth M
PROVIDER: S-EPMC2576293 | biostudies-literature | 2006 Apr
REPOSITORIES: biostudies-literature
Howarth Mark M Chinnapen Daniel J-F DJ Gerrow Kimberly K Dorrestein Pieter C PC Grandy Melanie R MR Kelleher Neil L NL El-Husseini Alaa A Ting Alice Y AY
Nature methods 20060401 4
Streptavidin and avidin are used ubiquitously because of the remarkable affinity of their biotin binding, but they are tetramers, which disrupts many of their applications. Making either protein monomeric reduces affinity by at least 10(4)-fold because part of the binding site comes from a neighboring subunit. Here we engineered a streptavidin tetramer with only one functional biotin binding subunit that retained the affinity, off rate and thermostability of wild-type streptavidin. In denaturant ...[more]