PSS
PSS engineers water‑soluble α‑helical transmembrane proteins by applying the QTY/NTY amino‑acid substitution codes to enhance solubility while preserving native transmembrane helical structure.
Key Features:
- QTY/NTY Methodology: Implements the QTY and NTY amino‑acid substitution codes to replace hydrophobic residues with more polar residues to increase solubility while aiming to maintain α‑helical transmembrane conformation.
- Simple Design Model: Generates individual protein designs with typical computation times of approximately 2–4 minutes depending on target size and complexity.
- Library Design Module: Produces comprehensive variant libraries for targets with multiple transmembrane helices with typical computation times of approximately 2–5 hours.
- Protocols for Experimental Implementation: Provides protocols that describe how to apply QTY/NTY substitutions experimentally to translate designed sequences into biochemical studies.
Scientific Applications:
- Membrane protein solubility enhancement: Produces soluble variants of α‑helical transmembrane proteins to facilitate downstream biochemical and biophysical characterization.
- GPCR expression and purification: Enables design of water‑soluble variants of G‑protein coupled receptors to aid expression and purification for functional and structural studies.
- Experimental studies of membrane protein function: Supports generation of variants that can accelerate experimental workflows for probing biological roles of membrane proteins.
Methodology:
Performs systematic sequence design using the QTY/NTY codes to substitute specific amino acids, supported by computational algorithms to generate soluble transmembrane α‑helical variants while aiming to preserve native conformation.
Topics
Details
- Added:
- 11/14/2019
- Last Updated:
- 1/13/2021
Operations
Publications
Tao F, Tang H, Zhang S, Xu P. PSS: An enabling QTY server for designing water-soluble α-helical transmembrane proteins. Unknown Journal. 2019. doi:10.1101/724658.
DOI: 10.1101/724658