[Changes in the secondary and tertiary structure of serum albumin in interactions with ligands of various structures].

Abstract

High affinity interactions between blood serum albumin and five substances of various chemical structure, exhibiting distinct physiological activity, were accompanied by alterations in the protein tertiary structure, while the albumin secondary structure was involved in conformational transformation after less effective affinity binding.

Cite this paper

@article{Trinus1984ChangesIT, title={[Changes in the secondary and tertiary structure of serum albumin in interactions with ligands of various structures].}, author={F. P. Trinus and B S Braver-Chernobul'skaia and Alexander I. Luik and A E Boldeskul and Anna N. Velichko}, journal={Voprosy meditsinskoi khimii}, year={1984}, volume={30 4}, pages={48-50} }