Original paper
A ClpS-based N-terminal amino acid binding reagent with improved thermostability and selectivity
Abstract
Realization of binding reagents that can perform high-fidelity, sequential recognition and detection of amino acids is important for the success of many proposed approaches for single-molecule protein sequencing. Towards this purpose, a variant of the Agrobacterium tumefaciens protein ClpS was previously engineered with improved binding affinity for phenylalanine at the N-terminus of a peptide. In this study, this variant was further engineered...
Paper Details
Title
A ClpS-based N-terminal amino acid binding reagent with improved thermostability and selectivity
Published Date
Feb 1, 2020
Volume
154
Pages
107438 - 107438
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Notes
History