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Helix–coil transition of poly(α, L ‐glutamic acid) at an interface: Correlation with static and dynamic membrane properties
Author(s) -
Pefferkorn Emile,
Schmitt Adrien,
Varoqui Raphaël
Publication year - 1982
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360210713
Subject(s) - chemistry , helix (gastropod) , membrane , aqueous solution , cellulose acetate , adsorption , permeability (electromagnetism) , filter paper , electromagnetic coil , crystallography , biophysics , polymer chemistry , chromatography , biochemistry , ecology , snail , electrical engineering , biology , engineering
When adsorbed from an aqueous dilute solution at high pH into the pores of an inert cellulose acetate filter, poly(α, L ‐glutamic acid) remains strongly anchored to the pore walls. The existence of the helix–coil transition for the adsorbed polypeptide in a certain pH range is evidenced by static and dynamic membrane properties displayed by the “activated” filter, such as excess cation uptake, membrane potential, and hyraulic permeability. In particular, the variations of the hydrodynamic thickeness present a sigmoidal shape characteristic of the helix–coil transition at the interface, a transition apparently less sharp than in solution.