Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent

Cell cycle regulatory enzyme Pin1 both catalyzes pSer/Thr-<i>cis/trans</i>-Pro isomerization and binds the same motif separately in its WW domain. To better understand the function of Pin1, a way to separate these activities is needed. An unnatural peptide library, R<sup>1</sup&...

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Bibliographic Details
Main Author:	Xingguo R. Chen (19818734) (author)
Other Authors:	Ana Y. Mercedes-Camacho (1890403) (author), Kimberly A. Wilson (2303062) (author), Jill J. Bouchard (1301145) (author), Jeffrey W. Peng (236073) (author), Felicia A. Etzkorn (135144) (author)
Published:	2024
Subjects:	Biophysics Biochemistry Cell Biology Pharmacology Biotechnology Immunology Chemical Sciences not elsewhere classified phosphoramidite functional group phase phosphorylating reagent competitive dissociation constants >- pro isomerization unnatural peptide library 15 </ sup 1 </ sup identify ligands specific pin1 ww domain trans </ k </ </ sub ww domain wang resin thr -< shift perturbations parallel synthesis one step nmr chemical new solid motif separately member library ligands bound labeled pin1 final 315 easy solid catalyzes pser better understand best hits >< sub
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Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent

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