Autor: |
Huang J; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois 60637, USA., Nagy SS, Koide A, Rock RS, Koide S |
Jazyk: |
angličtina |
Zdroj: |
Biochemistry [Biochemistry] 2009 Dec 22; Vol. 48 (50), pp. 11834-6. |
DOI: |
10.1021/bi901756n |
Abstrakt: |
A peptide fusion tag and accompanying recombinant capture reagents have been developed on the basis of the peptide-PDZ domain interaction and affinity clamps, a new class of affinity reagent. This system allows for single-step purification under mild conditions and stable capture of a tagged protein. The subnanomolar affinity, high force resistance (>30 pN), small size ( approximately 25 kDa, approximately one-sixth of the size of IgG), and monomeric nature of the affinity clamp are all superior features for many applications, in particular single-molecule measurements. |
Databáze: |
MEDLINE |
Externí odkaz: |
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