Affinity Partitioning Using Poly(ethylene glycol) with Covalently Coupled Hydrophobic Groups
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Many biological processes, such as regulation, catalysis, and complex formation, depend on the capacity of biopolymers to interact with apolar groups, i.e., their surface or “effective” hydrophobicity (1 ). The determination of surface hydrophobicity is therefore important for understanding the mechanism of interaction of a biopolymer with its ligands. The determination of surface hydrophobicity is also important for designing a method for the purification or the concentration of biopolymers, especially proteins.
![EIN2抗体EIN2一抗抗体Ethylene-insensitive protein 2 (AtEIN2) (EIN-2) (Cytokinin-resistant protein AtCKR1) (Protein ORESARA 3) [Cleaved into: EIN2-CEND (EIN2C)] EIN2 CKR1 ORE3 At5g03280 F12E4.10 MOK16.19抗体EIN2 Antibody抗体](https://img1.dxycdn.com/p/s14/2024/0814/834/6121613515047163281.jpg!wh200)
